Peptides composed of between two and twelve amino acids.
Peptides that inhibit mitosis (ANTIMITOTICS). During the 1960's the term referred to crude extracts that inhibited cell proliferation; the activity was later attributed to PYROGLUTAMATE type oligopeptides.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The simplest of all peptides. It functions as a gamma-glutamyl acceptor.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Peptides composed of two amino acid units.
A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A semisynthetic cephalosporin antibiotic with antimicrobial activity similar to that of CEPHALORIDINE or CEPHALOTHIN, but somewhat less potent. It is effective against both gram-positive and gram-negative organisms.
Antibodies that can catalyze a wide variety of chemical reactions. They are characterized by high substrate specificity and share many mechanistic features with enzymes.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
The process of cleaving a chemical compound by the addition of a molecule of water.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
A non-pathogenic species of LACTOCOCCUS found in DAIRY PRODUCTS and responsible for the souring of MILK and the production of LACTIC ACID.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
A zinc containing enzyme of the hydrolase class that catalyzes the removal of the N-terminal amino acid from most L-peptides, particularly those with N-terminal leucine residues but not those with N-terminal lysine or arginine residues. This occurs in tissue cell cytosol, with high activity in the duodenum, liver, and kidney. The activity of this enzyme is commonly assayed using a leucine arylamide chromogenic substrate such as leucyl beta-naphthylamide.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
The rate dynamics in chemical or physical systems.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Uptake of substances through the lining of the INTESTINES.
A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An essential amino acid. It is often added to animal feed.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Sites on an antigen that interact with specific antibodies.
Proteins prepared by recombinant DNA technology.
Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.
Transport proteins that carry specific substances in the blood or across cell membranes.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
The sum of the weight of all the atoms in a molecule.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
Proteins found in any species of bacterium.
Stable elementary particles having the smallest known positive charge, found in the nuclei of all elements. The proton mass is less than that of a neutron. A proton is the nucleus of the light hydrogen atom, i.e., the hydrogen ion.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Established cell cultures that have the potential to propagate indefinitely.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
Proteins found in any species of virus.
Substances elaborated by viruses that have antigenic activity.
Immunoglobulins produced in response to VIRAL ANTIGENS.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Antibodies produced by a single clone of cells.
The relationship between the dose of an administered drug and the response of the organism to the drug.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).

Inhibition of in vitro enteric neuronal development by endothelin-3: mediation by endothelin B receptors. (1/10855)

The terminal colon is aganglionic in mice lacking endothelin-3 or its receptor, endothelin B. To analyze the effects of endothelin-3/endothelin B on the differentiation of enteric neurons, E11-13 mouse gut was dissociated, and positive and negative immunoselection with antibodies to p75(NTR )were used to isolate neural crest- and non-crest-derived cells. mRNA encoding endothelin B was present in both the crest-and non-crest-derived cells, but that encoding preproendothelin-3 was detected only in the non-crest-derived population. The crest- and non-crest-derived cells were exposed in vitro to endothelin-3, IRL 1620 (an endothelin B agonist), and/or BQ 788 (an endothelin B antagonist). Neurons and glia developed only in cultures of crest-derived cells, and did so even when endothelin-3 was absent and BQ 788 was present. Endothelin-3 inhibited neuronal development, an effect that was mimicked by IRL 1620 and blocked by BQ 788. Endothelin-3 failed to stimulate the incorporation of [3H]thymidine or bromodeoxyuridine. Smooth muscle development in non-crest-derived cell cultures was promoted by endothelin-3 and inhibited by BQ 788. In contrast, transcription of laminin alpha1, a smooth muscle-derived promoter of neuronal development, was inhibited by endothelin-3, but promoted by BQ 788. Neurons did not develop in explants of the terminal bowel of E12 ls/ls (endothelin-3-deficient) mice, but could be induced to do so by endothelin-3 if a source of neural precursors was present. We suggest that endothelin-3/endothelin B normally prevents the premature differentiation of crest-derived precursors migrating to and within the fetal bowel, enabling the precursor population to persist long enough to finish colonizing the bowel.  (+info)

Primary haemostasis: sticky fingers cement the relationship. (2/10855)

Platelet aggregation to form a haemostatic plug, or thrombus, plays a key role in preventing bleeding from a wound. Recent studies have provided new insights into how platelet receptors are deployed during the interactions with the vascular subendothelial matrix that lead to haemostatic plug formation.  (+info)

Bcl-2 regulates amplification of caspase activation by cytochrome c. (3/10855)

Caspases, a family of specific proteases, have central roles in apoptosis [1]. Caspase activation in response to diverse apoptotic stimuli involves the relocalisation of cytochrome c from mitochondria to the cytoplasm where it stimulates the proteolytic processing of caspase precursors. Cytochrome c release is controlled by members of the Bcl-2 family of apoptosis regulators [2] [3]. The anti-apoptotic members Bcl-2 and Bcl-xL may also control caspase activation independently of cytochrome c relocalisation or may inhibit a positive feedback mechanism [4] [5] [6] [7]. Here, we investigate the role of Bcl-2 family proteins in the regulation of caspase activation using a model cell-free system. We found that Bcl-2 and Bcl-xL set a threshold in the amount of cytochrome c required to activate caspases, even in soluble extracts lacking mitochondria. Addition of dATP (which stimulates the procaspase-processing factor Apaf-1 [8] [9]) overcame inhibition of caspase activation by Bcl-2, but did not prevent the control of cytochrome c release from mitochondria by Bcl-2. Cytochrome c release was accelerated by active caspase-3 and this positive feedback was negatively regulated by Bcl-2. These results provide evidence for a mechanism to amplify caspase activation that is suppressed at several distinct steps by Bcl-2, even after cytochrome c is released from mitochondria.  (+info)

C/EBPalpha regulates generation of C/EBPbeta isoforms through activation of specific proteolytic cleavage. (4/10855)

C/EBPalpha and C/EBPbeta are intronless genes that can produce several N-terminally truncated isoforms through the process of alternative translation initiation at downstream AUG codons. C/EBPbeta has been reported to produce four isoforms: full-length 38-kDa C/EBPbeta, 35-kDa LAP (liver-enriched transcriptional activator protein), 21-kDa LIP (liver-enriched transcriptional inhibitory protein), and a 14-kDa isoform. In this report, we investigated the mechanisms by which C/EBPbeta isoforms are generated in the liver and in cultured cells. Using an in vitro translation system, we found that LIP can be generated by two mechanisms: alternative translation and a novel mechanism-specific proteolytic cleavage of full-length C/EBPbeta. Studies of mice in which the C/EBPalpha gene had been deleted (C/EBPalpha-/-) showed that the regulation of C/EBPbeta proteolysis is dependent on C/EBPalpha. The induction of C/EBPalpha in cultured cells leads to induced cleavage of C/EBPbeta to generate the LIP isoform. We characterized the cleavage activity in mouse liver extracts and found that the proteolytic cleavage activity is specific to prenatal and newborn livers, is sensitive to chymostatin, and is completely abolished in C/EBPalpha-/- animals. The lack of cleavage activity in the livers of C/EBPalpha-/- mice correlates with the decreased levels of LIP in the livers of these animals. Analysis of LIP production during liver regeneration showed that, in this system, the transient induction of LIP is dependent on the third AUG codon and most likely involves translational control. We propose that there are two mechanisms by which C/EBPbeta isoforms might be generated in the liver and in cultured cells: one that is determined by translation and a second that involves C/EBPalpha-dependent, specific proteolytic cleavage of full-length C/EBPbeta. The latter mechanism implicates C/EBPalpha in the regulation of posttranslational generation of the dominant negative C/EBPbeta isoform, LIP.  (+info)

Crystal structures of two H-2Db/glycopeptide complexes suggest a molecular basis for CTL cross-reactivity. (5/10855)

Two synthetic O-GlcNAc-bearing peptides that elicit H-2Db-restricted glycopeptide-specific cytotoxic T cells (CTL) have been shown to display nonreciprocal patterns of cross-reactivity. Here, we present the crystal structures of the H-2Db glycopeptide complexes to 2.85 A resolution or better. In both cases, the glycan is solvent exposed and available for direct recognition by the T cell receptor (TCR). We have modeled the complex formed between the MHC-glycopeptide complexes and their respective TCRs, showing that a single saccharide residue can be accommodated in the standard TCR-MHC geometry. The models also reveal a possible molecular basis for the observed cross-reactivity patterns of the CTL clones, which appear to be influenced by the length of the CDR3 loop and the nature of the immunizing ligand.  (+info)

Role of endothelin in the increased vascular tone of patients with essential hypertension. (6/10855)

We investigated the possible role of endothelin in the increased vasoconstrictor tone of hypertensive patients using antagonists of endothelin receptors. Forearm blood flow (FBF) responses (strain-gauge plethysmography) to intraarterial infusion of blockers of endothelin-A (ETA) (BQ-123) and endothelin-B (ETB) (BQ-788) receptors, separately and in combination, were measured in hypertensive patients and normotensive control subjects. In healthy subjects, BQ-123 alone or in combination with BQ-788 did not significantly modify FBF (P=0.78 and P=0.63, respectively). In hypertensive patients, in contrast, BQ-123 increased FBF by 33+/-7% (P<0.001 versus baseline), and the combination of BQ-123 and BQ-788 resulted in a greater vasodilator response (63+/-12%; P=0.006 versus BQ-123 alone in the same subjects). BQ-788 produced a divergent vasoactive effect in the two groups, with a decrease of FBF (17+/-5%; P=0.004 versus baseline) in control subjects and transient vasodilation (15+/-7% after 20 minutes) in hypertensive patients (P<0.001, hypertensives versus controls). The vasoconstrictor response to endothelin-1 was slightly higher (P=0.04) in hypertensive patients (46+/-4%) than in control subjects (32+/-4%). Our data indicate that patients with essential hypertension have increased vascular endothelin activity, which may be of pathophysiological relevance to their increased vascular tone. In these patients, nonselective ETA and ETB blockade seems to produce a greater vasodilator effect than selective ETA blockade.  (+info)

99mTc-labeled vasoactive intestinal peptide receptor agonist: functional studies. (7/10855)

Vasoactive intestinal peptide (VIP) is a naturally occurring 28-amino acid peptide with a wide range of biological activities. Recent reports suggest that VIP receptors are expressed on a variety of malignant tumor cells and that the receptor density is higher than for somatostatin. Our aims were to label VIP with 99mTc--a generator-produced, inexpensive radionuclide that possesses ideal characteristics for scintigraphic imaging--and to evaluate 99mTc-VIP for bioactivity and its ability to detect experimental tumors. METHODS: VIP28 was modified at the carboxy terminus by the addition of four amino acids that provided an N4 configuration for a strong chelation of 99mTc. To eliminate steric hindrance, 4-aminobutyric acid (Aba) was used as a spacer. VIP28 was labeled with 1251, which served as a control. Biological activity of the modified VIP28 agonist (TP3654) was examined in vitro using a cell-binding assay and an opossum internal anal sphincter (IAS) smooth muscle relaxivity assay. Tissue distribution studies were performed at 4 and 24 h after injection, and receptor-blocking assays were also performed in nude mice bearing human colorectal cancer LS174T. Blood clearance was examined in normal Sprague-Dawley rats. RESULTS: The yield of 99mTc-TP3654 was quantitative, and the yields of 125I-VIP and 1251-TP3654 were >90%. All in vitro data strongly suggested that the biological activity of 99mTc-TP3654 agonist was equivalent to that of VIP28. As the time after injection increased, radioactivity in all tissues decreased, except in the receptor-enriched tumor (P = 0.84) and in the lungs (P = 0.78). The tumor uptake (0.23 percentage injected dose per gram of tissue [%ID/g]) was several-fold higher than 125I-VIP (0.06 %ID/g) at 24 h after injection in the similar system. In mice treated with unlabeled VIP or TP3654, the uptake of 99mTc-TP3654 decreased in all VIP receptor-rich tissues except the kidneys. The blood clearance was biphasic; the alpha half-time was 5 min and the beta half-time was approximately 120 min. CONCLUSION: VIP28 was modified and successfully labeled with 99mTc. The results of all in vitro examinations indicated that the biological activity of TP3654 was equivalent to that of native VIP28 and tumor binding was receptor specific.  (+info)

Stimulation of phosphorylase kinase autophosphorylation by peptide analogs of phosphorylase. (8/10855)

Autoactivation of phosphorylase kinase in the presence of substrates has been studied to determine the cause of the hysteresis, or lag, in the phosphorylase kinase reaction. Peptide analogs corresponding to the convertible serine region of phosphorylase have been used as low molecular weight alternative substrates. Autophosphorylation of the kinase molecule was measured under conditions that favored autoactivation. Phosphorylase b and a tetradecapeptide, which was found to be a good model of phosphorylase, stimulated autoactivation by 86- and 37-fold, respectively. The tetradecapeptide also stimulated autophosphorylation of subunits A and B of the kinase molecule. This increased autophosphorylation coincided with an increased ability to convert phosphorylase. This finding supports the hypothesis that autophosphorylation is responsible for the lag in the phosphorylase kinase reaction. No evidence was obtained to suggest that the lag could be due to dissociation of the kinase. The stoichiometry of phosphate incorporation into phosphorylase kinase subunits by autophosphorylation was much greater than that reported to occur by protein kinase phosphorylation. Multiple phosphorylation sites in subunit A accounted for most of the phosphate incorporation during autophosphorylation. Saturating levels of hexa- and octapeptide analogs also caused stimulation of autophosphorylation. Possible mechanisms and experimental implications of substrate-stimulated autophosphorylation are discussed. Consideration also is given to the possible role of effectors in autophosphorylation in vivo.  (+info)

Oligopeptides are defined in medicine and biochemistry as short chains of amino acids, typically containing fewer than 20 amino acid residues. These small peptides are important components in various biological processes, such as serving as signaling molecules, enzyme inhibitors, or structural elements in some proteins. They can be found naturally in foods and may also be synthesized for use in medical research and therapeutic applications.

Chalones are hypothetical substances that were once thought to regulate the growth and proliferation of cells, particularly in the context of wound healing. The concept of chalones was first introduced in the 1950s by British scientist Dr. G. Kingsley Noble, who proposed that these substances might be produced by cells themselves and released into the extracellular environment to inhibit further cell division.

The idea behind chalones was that they might provide a natural mechanism for controlling the growth of tissues and preventing unregulated cell proliferation, which could lead to cancer. However, despite extensive research, no definitive evidence has been found to support the existence of chalones as distinct molecular entities.

While the concept of chalones has largely fallen out of favor in modern scientific discourse, the idea of using naturally occurring or synthetic molecules to regulate cell growth and proliferation remains an active area of research in fields such as cancer therapy and tissue engineering.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Glycylglycine is not a medical condition or term, but rather it is a chemical compound. It is a dipeptide, which means it is composed of two amino acids linked together. Specifically, glycylglycine consists of two glycine molecules joined by an amide bond (also known as a peptide bond) between the carboxyl group of one glycine and the amino group of the other glycine.

Glycylglycine is often used in laboratory research as a buffer, a substance that helps maintain a stable pH level in a solution. It has a relatively simple structure and is not naturally found in significant amounts in living organisms.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

A dipeptide is a type of molecule that is formed by the condensation of two amino acids. In this process, the carboxyl group (-COOH) of one amino acid combines with the amino group (-NH2) of another amino acid, releasing a water molecule and forming a peptide bond.

The resulting molecule contains two amino acids joined together by a single peptide bond, which is a type of covalent bond that forms between the carboxyl group of one amino acid and the amino group of another. Dipeptides are relatively simple molecules compared to larger polypeptides or proteins, which can contain hundreds or even thousands of amino acids linked together by multiple peptide bonds.

Dipeptides have a variety of biological functions in the body, including serving as building blocks for larger proteins and playing important roles in various physiological processes. Some dipeptides also have potential therapeutic uses, such as in the treatment of hypertension or muscle wasting disorders.

Aminopeptidases are a group of enzymes that catalyze the removal of amino acids from the N-terminus of polypeptides and proteins. They play important roles in various biological processes, including protein degradation, processing, and activation. Aminopeptidases are classified based on their specificity for different types of amino acids and the mechanism of their action. Some of the well-known aminopeptidases include leucine aminopeptidase, alanyl aminopeptidase, and arginine aminopeptidase. They are widely distributed in nature and found in various tissues and organisms, including bacteria, plants, and animals. In humans, aminopeptidases are involved in several physiological functions, such as digestion, immune response, and blood pressure regulation.

Peptides are short chains of amino acid residues linked by covalent bonds, known as peptide bonds. They are formed when two or more amino acids are joined together through a condensation reaction, which results in the elimination of a water molecule and the formation of an amide bond between the carboxyl group of one amino acid and the amino group of another.

Peptides can vary in length from two to about fifty amino acids, and they are often classified based on their size. For example, dipeptides contain two amino acids, tripeptides contain three, and so on. Oligopeptides typically contain up to ten amino acids, while polypeptides can contain dozens or even hundreds of amino acids.

Peptides play many important roles in the body, including serving as hormones, neurotransmitters, enzymes, and antibiotics. They are also used in medical research and therapeutic applications, such as drug delivery and tissue engineering.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Cephalexin is a type of antibiotic known as a first-generation cephalosporin. It works by interfering with the bacteria's ability to form a cell wall, which is essential for its survival. Without a functional cell wall, the bacterial cells become unstable and eventually die.

Cephalexin is effective against a wide range of gram-positive and some gram-negative bacteria, making it a useful antibiotic for treating various types of infections, such as respiratory tract infections, skin and soft tissue infections, bone and joint infections, and urinary tract infections.

Like all antibiotics, cephalexin should be used only to treat bacterial infections, as it has no effect on viral infections. It is important to take the full course of treatment as directed by a healthcare professional, even if symptoms improve before the medication is finished, to ensure that the infection is fully treated and to reduce the risk of antibiotic resistance.

Common side effects of cephalexin include nausea, diarrhea, vomiting, and stomach pain. In rare cases, more serious side effects such as allergic reactions, severe skin rashes, or liver damage may occur. It is important to seek medical attention immediately if any signs of an allergic reaction or serious side effect are experienced while taking cephalexin.

Catalytic antibodies, also known as abzymes or catalytic immune proteins, are a type of antibody that possesses enzymatic activity. They are capable of accelerating specific chemical reactions in a manner similar to traditional enzymes. This unique property arises from the ability of certain antibodies to bind substrates and promote their conversion into products through a series of chemical transformations.

Catalytic antibodies are generated by immunizing an organism with a transition state analogue, a molecule that mimics the high-energy, transient structure of a substrate during a chemical reaction. The immune system recognizes this analogue as foreign and produces antibodies against it. Some of these antibodies will bind to the transition state analogue in a way that stabilizes its geometry and lowers the energy barrier for the conversion of the substrate into the product. This results in the formation of a catalytic antibody, which can then accelerate this specific chemical reaction when presented with the appropriate substrate.

These specialized antibodies have attracted significant interest in the fields of chemistry, biochemistry, and immunology due to their potential applications in various areas, including drug design, diagnostics, and environmental monitoring. However, it is important to note that catalytic antibodies are still a subject of ongoing research, and their use as practical tools in these applications is not yet widespread.

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

Hydrolysis is a chemical process, not a medical one. However, it is relevant to medicine and biology.

Hydrolysis is the breakdown of a chemical compound due to its reaction with water, often resulting in the formation of two or more simpler compounds. In the context of physiology and medicine, hydrolysis is a crucial process in various biological reactions, such as the digestion of food molecules like proteins, carbohydrates, and fats. Enzymes called hydrolases catalyze these hydrolysis reactions to speed up the breakdown process in the body.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

"Lactococcus lactis" is a species of gram-positive, facultatively anaerobic bacteria that are commonly found in nature, particularly in environments involving plants and dairy products. It is a catalase-negative, non-spore forming coccus that typically occurs in pairs or short chains.

"Lactococcus lactis" has significant industrial importance as it plays a crucial role in the production of fermented foods such as cheese and buttermilk. The bacterium converts lactose into lactic acid, which contributes to the sour taste and preservative qualities of these products.

In addition to its use in food production, "Lactococcus lactis" has been explored for its potential therapeutic applications. It can be used as a vector for delivering therapeutic proteins or vaccines to the gastrointestinal tract due to its ability to survive and colonize there.

It's worth noting that "Lactococcus lactis" is generally considered safe for human consumption, and it's one of the most commonly used probiotics in food and supplements.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

Leucyl aminopeptidase (LAP) is an enzyme that plays a role in the metabolism and breakdown of proteins. It is found in various tissues and organs throughout the body, including the small intestine, liver, and kidneys. LAP specifically catalyzes the removal of leucine, a type of amino acid, from the N-terminus (the beginning) of peptides and proteins. This enzyme is important for the proper digestion and absorption of dietary proteins, as well as for the regulation of various physiological processes in the body. Abnormal levels or activity of LAP have been implicated in certain diseases, such as cancer and liver disease.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Alanine is an alpha-amino acid that is used in the biosynthesis of proteins. The molecular formula for alanine is C3H7NO2. It is a non-essential amino acid, which means that it can be produced by the human body through the conversion of other nutrients, such as pyruvate, and does not need to be obtained directly from the diet.

Alanine is classified as an aliphatic amino acid because it contains a simple carbon side chain. It is also a non-polar amino acid, which means that it is hydrophobic and tends to repel water. Alanine plays a role in the metabolism of glucose and helps to regulate blood sugar levels. It is also involved in the transfer of nitrogen between tissues and helps to maintain the balance of nitrogen in the body.

In addition to its role as a building block of proteins, alanine is also used as a neurotransmitter in the brain and has been shown to have a calming effect on the nervous system. It is found in many foods, including meats, poultry, fish, eggs, dairy products, and legumes.

Protease inhibitors are a class of antiviral drugs that are used to treat infections caused by retroviruses, such as the human immunodeficiency virus (HIV), which is responsible for causing AIDS. These drugs work by blocking the activity of protease enzymes, which are necessary for the replication and multiplication of the virus within infected cells.

Protease enzymes play a crucial role in the life cycle of retroviruses by cleaving viral polyproteins into functional units that are required for the assembly of new viral particles. By inhibiting the activity of these enzymes, protease inhibitors prevent the virus from replicating and spreading to other cells, thereby slowing down the progression of the infection.

Protease inhibitors are often used in combination with other antiretroviral drugs as part of highly active antiretroviral therapy (HAART) for the treatment of HIV/AIDS. Common examples of protease inhibitors include saquinavir, ritonavir, indinavir, and atazanavir. While these drugs have been successful in improving the outcomes of people living with HIV/AIDS, they can also cause side effects such as nausea, diarrhea, headaches, and lipodystrophy (changes in body fat distribution).

Biological transport refers to the movement of molecules, ions, or solutes across biological membranes or through cells in living organisms. This process is essential for maintaining homeostasis, regulating cellular functions, and enabling communication between cells. There are two main types of biological transport: passive transport and active transport.

Passive transport does not require the input of energy and includes:

1. Diffusion: The random movement of molecules from an area of high concentration to an area of low concentration until equilibrium is reached.
2. Osmosis: The diffusion of solvent molecules (usually water) across a semi-permeable membrane from an area of lower solute concentration to an area of higher solute concentration.
3. Facilitated diffusion: The assisted passage of polar or charged substances through protein channels or carriers in the cell membrane, which increases the rate of diffusion without consuming energy.

Active transport requires the input of energy (in the form of ATP) and includes:

1. Primary active transport: The direct use of ATP to move molecules against their concentration gradient, often driven by specific transport proteins called pumps.
2. Secondary active transport: The coupling of the movement of one substance down its electrochemical gradient with the uphill transport of another substance, mediated by a shared transport protein. This process is also known as co-transport or counter-transport.

Dipeptidyl-peptidases (DPPs) and tripeptidyl-peptidases (TPPs) are two types of enzymes that belong to the class of peptidases, which are proteins that help break down other proteins into smaller peptides or individual amino acids.

Dipeptidyl-peptidases cleave dipeptides (two-amino acid units) from the N-terminus (the end with a free amino group) of polypeptides and proteins, while tripeptidyl-peptidases cleave tripeptides (three-amino acid units) from the same location.

There are several different isoforms of DPPs and TPPs that have been identified in various organisms, including humans. These enzymes play important roles in regulating various physiological processes, such as digestion, immune function, and blood glucose homeostasis.

Inhibitors of DPP-4, one specific isoform of DPPs, have been developed for the treatment of type 2 diabetes, as they help increase the levels of incretin hormones that stimulate insulin secretion and suppress glucagon production.

Proline is an organic compound that is classified as a non-essential amino acid, meaning it can be produced by the human body and does not need to be obtained through the diet. It is encoded in the genetic code as the codon CCU, CCC, CCA, or CCG. Proline is a cyclic amino acid, containing an unusual secondary amine group, which forms a ring structure with its carboxyl group.

In proteins, proline acts as a structural helix breaker, disrupting the alpha-helix structure and leading to the formation of turns and bends in the protein chain. This property is important for the proper folding and function of many proteins. Proline also plays a role in the stability of collagen, a major structural protein found in connective tissues such as tendons, ligaments, and skin.

In addition to its role in protein structure, proline has been implicated in various cellular processes, including signal transduction, apoptosis, and oxidative stress response. It is also a precursor for the synthesis of other biologically important compounds such as hydroxyproline, which is found in collagen and elastin, and glutamate, an excitatory neurotransmitter in the brain.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

Intestinal absorption refers to the process by which the small intestine absorbs water, nutrients, and electrolytes from food into the bloodstream. This is a critical part of the digestive process, allowing the body to utilize the nutrients it needs and eliminate waste products. The inner wall of the small intestine contains tiny finger-like projections called villi, which increase the surface area for absorption. Nutrients are absorbed into the bloodstream through the walls of the capillaries in these villi, and then transported to other parts of the body for use or storage.

Caseins are a group of phosphoproteins found in the milk of mammals, including cows and humans. They are the major proteins in milk, making up about 80% of the total protein content. Caseins are characterized by their ability to form micelles, or tiny particles, in milk when it is mixed with calcium. This property allows caseins to help transport calcium and other minerals throughout the body.

Caseins are also known for their nutritional value, as they provide essential amino acids and are easily digestible. They are often used as ingredients in infant formula and other food products. Additionally, caseins have been studied for their potential health benefits, such as reducing the risk of cardiovascular disease and improving bone health. However, more research is needed to confirm these potential benefits.

Peptide hydrolases, also known as proteases or peptidases, are a group of enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes such as protein degradation, digestion, cell signaling, and regulation of various physiological functions. Based on their catalytic mechanism and the specificity for the peptide bond, they are classified into several types, including serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. These enzymes have important clinical applications in the diagnosis and treatment of various diseases, such as cancer, viral infections, and inflammatory disorders.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Glycine is a simple amino acid that plays a crucial role in the body. According to the medical definition, glycine is an essential component for the synthesis of proteins, peptides, and other biologically important compounds. It is also involved in various metabolic processes, such as the production of creatine, which supports muscle function, and the regulation of neurotransmitters, affecting nerve impulse transmission and brain function. Glycine can be found as a free form in the body and is also present in many dietary proteins.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Biological transport, active is the process by which cells use energy to move materials across their membranes from an area of lower concentration to an area of higher concentration. This type of transport is facilitated by specialized proteins called transporters or pumps that are located in the cell membrane. These proteins undergo conformational changes to physically carry the molecules through the lipid bilayer of the membrane, often against their concentration gradient.

Active transport requires energy because it works against the natural tendency of molecules to move from an area of higher concentration to an area of lower concentration, a process known as diffusion. Cells obtain this energy in the form of ATP (adenosine triphosphate), which is produced through cellular respiration.

Examples of active transport include the uptake of glucose and amino acids into cells, as well as the secretion of hormones and neurotransmitters. The sodium-potassium pump, which helps maintain resting membrane potential in nerve and muscle cells, is a classic example of an active transporter.

Circular dichroism (CD) is a technique used in physics and chemistry to study the structure of molecules, particularly large biological molecules such as proteins and nucleic acids. It measures the difference in absorption of left-handed and right-handed circularly polarized light by a sample. This difference in absorption can provide information about the three-dimensional structure of the molecule, including its chirality or "handedness."

In more technical terms, CD is a form of spectroscopy that measures the differential absorption of left and right circularly polarized light as a function of wavelength. The CD signal is measured in units of millidegrees (mdeg) and can be positive or negative, depending on the type of chromophore and its orientation within the molecule.

CD spectra can provide valuable information about the secondary and tertiary structure of proteins, as well as the conformation of nucleic acids. For example, alpha-helical proteins typically exhibit a strong positive band near 190 nm and two negative bands at around 208 nm and 222 nm, while beta-sheet proteins show a strong positive band near 195 nm and two negative bands at around 217 nm and 175 nm.

CD spectroscopy is a powerful tool for studying the structural changes that occur in biological molecules under different conditions, such as temperature, pH, or the presence of ligands or other molecules. It can also be used to monitor the folding and unfolding of proteins, as well as the binding of drugs or other small molecules to their targets.

Lysine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. Its chemical formula is (2S)-2,6-diaminohexanoic acid. Lysine is necessary for the growth and maintenance of tissues in the body, and it plays a crucial role in the production of enzymes, hormones, and antibodies. It is also essential for the absorption of calcium and the formation of collagen, which is an important component of bones and connective tissue. Foods that are good sources of lysine include meat, poultry, fish, eggs, and dairy products.

Stereoisomerism is a type of isomerism (structural arrangement of atoms) in which molecules have the same molecular formula and sequence of bonded atoms, but differ in the three-dimensional orientation of their atoms in space. This occurs when the molecule contains asymmetric carbon atoms or other rigid structures that prevent free rotation, leading to distinct spatial arrangements of groups of atoms around a central point. Stereoisomers can have different chemical and physical properties, such as optical activity, boiling points, and reactivities, due to differences in their shape and the way they interact with other molecules.

There are two main types of stereoisomerism: enantiomers (mirror-image isomers) and diastereomers (non-mirror-image isomers). Enantiomers are pairs of stereoisomers that are mirror images of each other, but cannot be superimposed on one another. Diastereomers, on the other hand, are non-mirror-image stereoisomers that have different physical and chemical properties.

Stereoisomerism is an important concept in chemistry and biology, as it can affect the biological activity of molecules, such as drugs and natural products. For example, some enantiomers of a drug may be active, while others are inactive or even toxic. Therefore, understanding stereoisomerism is crucial for designing and synthesizing effective and safe drugs.

An epitope is a specific region on the surface of an antigen (a molecule that can trigger an immune response) that is recognized by an antibody, B-cell receptor, or T-cell receptor. It is also commonly referred to as an antigenic determinant. Epitopes are typically composed of linear amino acid sequences or conformational structures made up of discontinuous amino acids in the antigen. They play a crucial role in the immune system's ability to differentiate between self and non-self molecules, leading to the targeted destruction of foreign substances like viruses and bacteria. Understanding epitopes is essential for developing vaccines, diagnostic tests, and immunotherapies.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Membrane transport proteins are specialized biological molecules, specifically integral membrane proteins, that facilitate the movement of various substances across the lipid bilayer of cell membranes. They are responsible for the selective and regulated transport of ions, sugars, amino acids, nucleotides, and other molecules into and out of cells, as well as within different cellular compartments. These proteins can be categorized into two main types: channels and carriers (or pumps). Channels provide a passive transport mechanism, allowing ions or small molecules to move down their electrochemical gradient, while carriers actively transport substances against their concentration gradient, requiring energy usually in the form of ATP. Membrane transport proteins play a crucial role in maintaining cell homeostasis, signaling processes, and many other physiological functions.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Metalloendopeptidases are a type of enzymes that cleave peptide bonds in proteins, specifically at interior positions within the polypeptide chain. They require metal ions as cofactors for their catalytic activity, typically zinc (Zn2+) or cobalt (Co2+). These enzymes play important roles in various biological processes such as protein degradation, processing, and signaling. Examples of metalloendopeptidases include thermolysin, matrix metalloproteinases (MMPs), and neutrophil elastase.

Mass spectrometry (MS) is an analytical technique used to identify and quantify the chemical components of a mixture or compound. It works by ionizing the sample, generating charged molecules or fragments, and then measuring their mass-to-charge ratio in a vacuum. The resulting mass spectrum provides information about the molecular weight and structure of the analytes, allowing for identification and characterization.

In simpler terms, mass spectrometry is a method used to determine what chemicals are present in a sample and in what quantities, by converting the chemicals into ions, measuring their masses, and generating a spectrum that shows the relative abundances of each ion type.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

In the context of medicine, particularly in relation to cancer treatment, protons refer to positively charged subatomic particles found in the nucleus of an atom. Proton therapy, a type of radiation therapy, uses a beam of protons to target and destroy cancer cells with high precision, minimizing damage to surrounding healthy tissue. The concentrated dose of radiation is delivered directly to the tumor site, reducing side effects and improving quality of life during treatment.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Serine endopeptidases are a type of enzymes that cleave peptide bonds within proteins (endopeptidases) and utilize serine as the nucleophilic amino acid in their active site for catalysis. These enzymes play crucial roles in various biological processes, including digestion, blood coagulation, and programmed cell death (apoptosis). Examples of serine endopeptidases include trypsin, chymotrypsin, thrombin, and elastase.

Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Secondary protein structure refers to the local spatial arrangement of amino acid chains in a protein, typically described as regular repeating patterns held together by hydrogen bonds. The two most common types of secondary structures are the alpha-helix (α-helix) and the beta-pleated sheet (β-sheet). In an α-helix, the polypeptide chain twists around itself in a helical shape, with each backbone atom forming a hydrogen bond with the fourth amino acid residue along the chain. This forms a rigid rod-like structure that is resistant to bending or twisting forces. In β-sheets, adjacent segments of the polypeptide chain run parallel or antiparallel to each other and are connected by hydrogen bonds, forming a pleated sheet-like arrangement. These secondary structures provide the foundation for the formation of tertiary and quaternary protein structures, which determine the overall three-dimensional shape and function of the protein.

Viral proteins are the proteins that are encoded by the viral genome and are essential for the viral life cycle. These proteins can be structural or non-structural and play various roles in the virus's replication, infection, and assembly process. Structural proteins make up the physical structure of the virus, including the capsid (the protein shell that surrounds the viral genome) and any envelope proteins (that may be present on enveloped viruses). Non-structural proteins are involved in the replication of the viral genome and modulation of the host cell environment to favor viral replication. Overall, a thorough understanding of viral proteins is crucial for developing antiviral therapies and vaccines.

An antigen is any substance that can stimulate an immune response, particularly the production of antibodies. Viral antigens are antigens that are found on or produced by viruses. They can be proteins, glycoproteins, or carbohydrates present on the surface or inside the viral particle.

Viral antigens play a crucial role in the immune system's recognition and response to viral infections. When a virus infects a host cell, it may display its antigens on the surface of the infected cell. This allows the immune system to recognize and target the infected cells for destruction, thereby limiting the spread of the virus.

Viral antigens are also important targets for vaccines. Vaccines typically work by introducing a harmless form of a viral antigen to the body, which then stimulates the production of antibodies and memory T-cells that can recognize and respond quickly and effectively to future infections with the actual virus.

It's worth noting that different types of viruses have different antigens, and these antigens can vary between strains of the same virus. This is why there are often different vaccines available for different viral diseases, and why flu vaccines need to be updated every year to account for changes in the circulating influenza virus strains.

Antibodies, viral are proteins produced by the immune system in response to an infection with a virus. These antibodies are capable of recognizing and binding to specific antigens on the surface of the virus, which helps to neutralize or destroy the virus and prevent its replication. Once produced, these antibodies can provide immunity against future infections with the same virus.

Viral antibodies are typically composed of four polypeptide chains - two heavy chains and two light chains - that are held together by disulfide bonds. The binding site for the antigen is located at the tip of the Y-shaped structure, formed by the variable regions of the heavy and light chains.

There are five classes of antibodies in humans: IgA, IgD, IgE, IgG, and IgM. Each class has a different function and is distributed differently throughout the body. For example, IgG is the most common type of antibody found in the bloodstream and provides long-term immunity against viruses, while IgA is found primarily in mucous membranes and helps to protect against respiratory and gastrointestinal infections.

In addition to their role in the immune response, viral antibodies can also be used as diagnostic tools to detect the presence of a specific virus in a patient's blood or other bodily fluids.

I believe there may be some confusion in your question. "Rabbits" is a common name used to refer to the Lagomorpha species, particularly members of the family Leporidae. They are small mammals known for their long ears, strong legs, and quick reproduction.

However, if you're referring to "rabbits" in a medical context, there is a term called "rabbit syndrome," which is a rare movement disorder characterized by repetitive, involuntary movements of the fingers, resembling those of a rabbit chewing. It is also known as "finger-chewing chorea." This condition is usually associated with certain medications, particularly antipsychotics, and typically resolves when the medication is stopped or adjusted.

Temperature, in a medical context, is a measure of the degree of hotness or coldness of a body or environment. It is usually measured using a thermometer and reported in degrees Celsius (°C), degrees Fahrenheit (°F), or kelvin (K). In the human body, normal core temperature ranges from about 36.5-37.5°C (97.7-99.5°F) when measured rectally, and can vary slightly depending on factors such as time of day, physical activity, and menstrual cycle. Elevated body temperature is a common sign of infection or inflammation, while abnormally low body temperature can indicate hypothermia or other medical conditions.

An Enzyme-Linked Immunosorbent Assay (ELISA) is a type of analytical biochemistry assay used to detect and quantify the presence of a substance, typically a protein or peptide, in a liquid sample. It takes its name from the enzyme-linked antibodies used in the assay.

In an ELISA, the sample is added to a well containing a surface that has been treated to capture the target substance. If the target substance is present in the sample, it will bind to the surface. Next, an enzyme-linked antibody specific to the target substance is added. This antibody will bind to the captured target substance if it is present. After washing away any unbound material, a substrate for the enzyme is added. If the enzyme is present due to its linkage to the antibody, it will catalyze a reaction that produces a detectable signal, such as a color change or fluorescence. The intensity of this signal is proportional to the amount of target substance present in the sample, allowing for quantification.

ELISAs are widely used in research and clinical settings to detect and measure various substances, including hormones, viruses, and bacteria. They offer high sensitivity, specificity, and reproducibility, making them a reliable choice for many applications.

"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Monoclonal antibodies are a type of antibody that are identical because they are produced by a single clone of cells. They are laboratory-produced molecules that act like human antibodies in the immune system. They can be designed to attach to specific proteins found on the surface of cancer cells, making them useful for targeting and treating cancer. Monoclonal antibodies can also be used as a therapy for other diseases, such as autoimmune disorders and inflammatory conditions.

Monoclonal antibodies are produced by fusing a single type of immune cell, called a B cell, with a tumor cell to create a hybrid cell, or hybridoma. This hybrid cell is then able to replicate indefinitely, producing a large number of identical copies of the original antibody. These antibodies can be further modified and engineered to enhance their ability to bind to specific targets, increase their stability, and improve their effectiveness as therapeutic agents.

Monoclonal antibodies have several mechanisms of action in cancer therapy. They can directly kill cancer cells by binding to them and triggering an immune response. They can also block the signals that promote cancer growth and survival. Additionally, monoclonal antibodies can be used to deliver drugs or radiation directly to cancer cells, increasing the effectiveness of these treatments while minimizing their side effects on healthy tissues.

Monoclonal antibodies have become an important tool in modern medicine, with several approved for use in cancer therapy and other diseases. They are continuing to be studied and developed as a promising approach to treating a wide range of medical conditions.

A dose-response relationship in the context of drugs refers to the changes in the effects or symptoms that occur as the dose of a drug is increased or decreased. Generally, as the dose of a drug is increased, the severity or intensity of its effects also increases. Conversely, as the dose is decreased, the effects of the drug become less severe or may disappear altogether.

The dose-response relationship is an important concept in pharmacology and toxicology because it helps to establish the safe and effective dosage range for a drug. By understanding how changes in the dose of a drug affect its therapeutic and adverse effects, healthcare providers can optimize treatment plans for their patients while minimizing the risk of harm.

The dose-response relationship is typically depicted as a curve that shows the relationship between the dose of a drug and its effect. The shape of the curve may vary depending on the drug and the specific effect being measured. Some drugs may have a steep dose-response curve, meaning that small changes in the dose can result in large differences in the effect. Other drugs may have a more gradual dose-response curve, where larger changes in the dose are needed to produce significant effects.

In addition to helping establish safe and effective dosages, the dose-response relationship is also used to evaluate the potential therapeutic benefits and risks of new drugs during clinical trials. By systematically testing different doses of a drug in controlled studies, researchers can identify the optimal dosage range for the drug and assess its safety and efficacy.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

An oligopeptide, often just called peptide (oligo-, "a few"), consists of two to twenty amino acids and can include dipeptides ... Netropsin - A basic oligopeptide isolated from Streptomyces netropsis. It is cytotoxic and its strong, specific binding to A-T ... Antipain - An oligopeptide produced by various bacteria which acts as a protease inhibitor. Ceruletide - A specific decapeptide ... Pepstatins - N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid ...
... is the part of renal physiology that deals with the retrieval of filtered oligopeptides, ... Longer oligopeptides, such as angiotensin and glutathione are degraded by enzymes on the brush border, while shorter ones, such ...
... is a synthetic, pH controlled self-assembling peptide used for biomimetic mineralization e.g. for enamel ... P11-4 (INCI name Oligopeptide 104) consists of the natural occurring amino acids Glutamine, Glutamic acid, Phenylalanine, ... "European Commission database with information on cosmetic substances and ingredients". Oligopeptide 104. Retrieved 1 July 2015 ... Remineralisation of teeth Oligopeptide Biomimetic materials Fluoride Brunton, P.A.; Davies, R.P.W. (2 July 2013). "Treatment of ...
... oligopeptide(in) The 3 substrates of this enzyme are ATP, H2O, and oligopeptide, whereas its 3 products are ADP, phosphate, and ... In enzymology, an oligopeptide-transporting ATPase (EC is an enzyme that catalyzes the chemical reaction ATP + H2O + ... The systematic name of this enzyme class is ATP phosphohydrolase (oligopeptide-importing). This enzyme is also called ... of the oligopeptide permease of Salmonella typhimurium". Mol. Microbiol. 6 (1): 47-57. doi:10.1111/j.1365-2958.1992.tb00836.x. ...
The proton-dependent oligopeptide transporter (PTR) family of proteins is distinct from the ABC-type peptide transporters and ... As of this edit, this article uses content from "2.A.17 The Proton-dependent Oligopeptide Transporter (POT/PTR) Family", which ... Oligopeptide transporter, peptide:H+ symporter InterPro: IPR004768 Amino acid/peptide transporter InterPro: IPR005279 FP12591; ... Proteins of the Proton-dependent Oligopeptide Transporter (POT) Family (also called the PTR (peptide transport) family) are ...
Molecular dynamics of oligopeptides. 3. Maps of levels of free energy of modified dipeptides and dynamic correlation in amino ...
The cinchona alkaloids, certain oligopeptides. Synthetic catalysts derived from biomolecules. Hydrogen bonding catalysts, ...
... various N-formyl oligopeptides that, like FMLP, are either released by microbes and mitochondria or are analogs of those ... released by microbes and mitochondria; b) microbe-derived non-formyl oligopeptides; c) certain polypeptides that are associated ...
... oligopeptides such as N-Formylmethionine-leucyl-phenylalanine; and various proteins such as the amino acid 1 to 42 fragment of ...
Oligopeptide Fyles, Thomas Murray; Luong, Horace (2009). "Solid-phase synthesis of a library of linear oligoester ion-channels ...
PepT 1 is a solute carrier for oligopeptides. It functions in renal oligopeptide reabsorption and in the intestines in a proton ... Gonzalez DE, Covitz KM, Sadée W, Mrsny RJ (1998). "An oligopeptide transporter is expressed at high levels in the pancreatic ... Adibi SA (2003). "Regulation of expression of the intestinal oligopeptide transporter (Pept-1) in health and disease". Am. J. ... "Entrez Gene: SLC15A1 Solute carrier family 15 (oligopeptide transporter), member 1". Liang R, Fei YJ, Prasad PD, Ramamoorthy S ...
Array-based oligo-peptide scanning. Also known as overlapping peptide scan or pepscan analysis, this technique uses a library ... For example, an antibody against CD20 was mapped in a study using array-based oligo-peptide scanning, by combining non-adjacent ... of oligo-peptide sequences from overlapping and non-overlapping segments of a target protein, and tests for their ability to ...
... alpha-oligopeptides". The FEBS Journal. 273 (23): 5261-72. doi:10.1111/j.1742-4658.2006.05519.x. PMID 17064315. S2CID 84167461 ... beta-oligopeptides". Chemistry & Biodiversity. 3 (12): 1325-48. doi:10.1002/cbdv.200690136. PMID 17193247. S2CID 38292191. ... "Bacterial beta-peptidyl aminopeptidases with unique substrate specificities for beta-oligopeptides and mixed beta, ...
"NMR Signal Enhancement by Effective SABRE Labeling of Oligopeptides". Chemistry - A European Journal. 21 (36): 12616-12619. doi ... "Magnetic Resonance Signal Amplification by Reversible Exchange of Selective PyFALGEA Oligopeptide Ligands Towards Epidermal ...
One example is oligopeptide P11-4. In dental orthopedics and implants, a more traditional strategy to improve the density of ...
Of particular interest are cyclic oligopeptides with 8 aminoacid rings. The leaves are known to contain the flavonoids ...
The 3 most popular ways of visualizing the alpha-helical secondary structure of oligopeptide sequences are (1) a helical wheel ... Changes in binding orientation also occur for facially-organized oligopeptides. This pattern is especially common in ... oligopeptides readily adopt stable α-helical structure. Furthermore, crosslinks can be incorporated into peptides to ...
CSF is a five amino acid oligopeptide and is exported via the GSP pathway. CSF enters the cell through oligopeptide permeate ... ComX is a ten amino acid oligopeptide; it requires two co-components, ComP, an histidine kinase, and ComA, a cytoplasmic ...
Cooperman BS (2003). "Oligopeptide inhibition of class I ribonucleotide reductases". Biopolymers. 71 (2): 117-31. doi:10.1002/ ...
Tandem repeats of short oligopeptides that are rich in glycine, proline, serine or threonine are capable of forming flexible ... Thus, these two codons and their respective amino acids must have been constituents of the earliest oligopeptides, with a ... Trifonov, Edward N. (September 2009). "The origin of the genetic code and of the earliest oligopeptides". Research in ... the early genetic code may have also produced low complexity oligo-peptides from valine and leucine. However, later on, within ...
Trifonov, Edward N. (September 2009). "The origin of the genetic code and of the earliest oligopeptides". Research in ...
The trypsin found in pancreatin works to hydrolyze proteins into oligopeptides; amylase hydrolyzes starches into ...
The other two major groups are oligopeptides AIs in Gram-positive bacteria; and autoinducer-2 (AI-2), as a universal signal for ...
Cyclophilins catalyze the cis-trans isomerization of peptidylprolyl imide bonds in oligopeptides. They have been proposed to ...
An oligopeptide, angiotensin is a hormone and a dipsogen. It is derived from the precursor molecule angiotensinogen, a serum ...
1995). "Self-complementary oligopeptide matrices support mammalian cell attachment". Biomaterials. 16 (18): 1385-1393. doi: ... 1993). "Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane" (PDF). Proc. Natl. ...
Blanco, Celia; Hochberg, David (2012). "Homochiral oligopeptides by chiral amplification: interpretation of experimental data ...
Many oligopeptides that possess an N-Formylmethionine N-terminal residue such as the prototypical tripeptide N-Formylmethionine ... Early studies suggested that these formyl oligopeptides operated by a Receptor (biochemistry) mechanism. Accordingly, the human ... function by binding any one of a wide variety of ligands including not only certain N-Formylmethionine-containing oligopeptides ... a gene that when transfected into FMLP-unresponsive cells bestowed responsiveness to this and other N-formyl oligopeptides. ...
This enzyme catalyses the following chemical reaction Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly ...
Unlike some AHLs, however, most oligopeptides do not act as transcription factors themselves. The free-living bioluminescent ... Gram-positive bacteria that participate in quorum sensing typically use secreted oligopeptides as autoinducers. Peptide ... Whereas Gram-negative bacteria primarily use acylated homoserine lactones, Gram-positive bacteria generally use oligopeptides ...
An oligopeptide, often just called peptide (oligo-, "a few"), consists of two to twenty amino acids and can include dipeptides ... Netropsin - A basic oligopeptide isolated from Streptomyces netropsis. It is cytotoxic and its strong, specific binding to A-T ... Antipain - An oligopeptide produced by various bacteria which acts as a protease inhibitor. Ceruletide - A specific decapeptide ... Pepstatins - N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid ...
The Gene Ontology (GO) project is a collaborative effort to address the need for consistent descriptions of gene products across databases. You can use this browser to view terms, definitions, and term relationships in a hierarchical display. Links to summary annotated gene data at MGI are provided in Term Detail reports.
... ranging from oligopeptides for sensory properties and peptides for hair, to a dandruff treatment and colorless carotenoids for ... Oligopeptides in Sensory, Proteins in Winter Skin and Carotenoids: Literature Findings. Jun 20th, 2013 ... ranging from oligopeptides for sensory properties and peptides for hair, to a dandruff treatment and colorless carotenoids for ...
Tetraplatinated artificial oligopeptides afford high affinity intercalation into dsDNA. In: Journal of the American Chemical ... Tetraplatinated artificial oligopeptides afford high affinity intercalation into dsDNA. Lauren A. Levine, Christopher M. Morgan ... Levine, L. A., Morgan, C. M., Ohr, K., & Williams, M. E. (2005). Tetraplatinated artificial oligopeptides afford high affinity ... Tetraplatinated artificial oligopeptides afford high affinity intercalation into dsDNA. Journal of the American Chemical ...
Collagen TripeptidesMarine collagen peptidesMarine fish oligopeptideTuna peptideOyster PeptidesCorn Protein Peptides ...
Tag Archives: oligopeptide synthesis. small molecule library is productive to T (HLA-DR+) cells in orthotopic tumor. Posted on ... Posted in Uncategorized , Tagged antigen peptide, fluorescent peptides, large-scale peptide synthesis, LY364947, oligopeptide ... Posted in Uncategorized , Tagged antigen peptide, fluorescent peptides, large-scale peptide synthesis, LY364947, oligopeptide ... Posted in Uncategorized , Tagged antigen peptide, fluorescent peptides, large-scale peptide synthesis, LY364947, oligopeptide ...
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Products with Oligopeptide-68. KLM Tyrolite Cream Kitoderm Glowing White Serum Libra Cosmetica Therapy Be White Elyns Lab ... Description: oligopeptide-68 is the synthetic peptide containing 12 amino acids consisting of arginine, aspartic acid, glycine ... As for research, we found one study from 2016 that combined Oligopeptide-68 with sunscreen and another skin-lightening active ... Overall, if you are into skin-lightening or fading pigmentation spots, Oligopeptide-68 might be something to try. ...
Oligopeptide miracle repair serum mask. Repair skin, reduce acne marks. Repair composition can solve dry, rough, acne and other ... Oligopeptide miracle repair serum mask. Repair skin, reduce acne marks. Repair composition can solve dry, rough, acne and other ... oligopeptide-I, oligopeptide-2, carbomer, triethanolamine, caprylhydroxamic acid, hydroxyacetophenone, peg-40 hydrogenated ... Benefits : Oligopeptide miracle repair serum mask. Repair skin, reduce acne marks. Repair composition can solve dry, rough, ...
This acne toner with variety of oligopeptides and plant extracts is gentle and non-irritating, and it can be absorbed quickly. ... Product Name: LANBENA Oligopeptides Acne Treatment Toner. Product Number: LB5774. Net Weight: 3.4fl oz / 100 ml. Shelf Life: 3 ... Product Efficacy: This acne toner with a variety of oligopeptides and plant extracts is gentle and non-irritating, and it can ... Product Efficacy: This acne toner with a variety of oligopeptides and plant extracts is gentle and non-irritating, and it can ...
This acne toner with variety of oligopeptides and plant extracts is gentle and non-irritating, and it can be absorbed quickly. ... Product Name: LANBENA Oligopeptides Acne Treatment Toner. Product Number: LB5774. Net Weight: 3.4fl oz / 100 ml. Shelf Life: 3 ... Product Efficacy: This acne toner with a variety of oligopeptides and plant extracts is gentle and non-irritating, and it can ... Product Efficacy: This acne toner with a variety of oligopeptides and plant extracts is gentle and non-irritating, and it can ...
Oligopeptide-34 is the most effective, non-hydroquinone ski ... Oligopeptide-34 is the most effective, non-hydroquinone skin ... Oligopeptide-34 decreases melanin synthesis and tyrosinase enzyme activity in melanocytes, decreasing the transfer of ... Oligopeptide-34 - a synthetically manufactured peptide containing 13 amino acids (including arginine). ... Oligopeptide-34 - a synthetically manufactured peptide containing 13 amino acids (including arginine). Oligopeptide-34 ...
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Smacin Composite Oligopeptide Prebiotics has anti cancer, anti inflammatory properties, fights leukaemia, diabetes, heart ... Norland Micromolecule Oligopeptide. ₦24,000.00. ₦23,500.00. Add to cart. * Sale! Longrich Vintage Wine. ₦17,000.00. ₦15,000.00 ...
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Branched Oligopeptides Form Nanocapsules with Lipid Vesicle Characteristics. Home » Branched Oligopeptides Form Nanocapsules ... TITLE: Branched Oligopeptides Form Nanocapsules with Lipid Vesicle Characteristics. Authors: Pinakin Sukthankar, Sushanth ...
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... Description. Glutathione Bulk powder is a tripeptide that contains an unusual ... and makes unremitting efforts to build the first brand of Lowest Price Anti-Wrinkle Oligopeptide-1 Powder. Through years of ...
... youthful-looking skin with Oligopeptides and what Oligopeptides can do for you. Visit Ice secret Blogs to know more! ... What Oligopeptides Can Do For You And Why You Want Them In Your ​​Skincare. Regarding skincare, oligopeptides are prized ... What Oligopeptides Do For Your Skin Oligopeptides are short sequences of amino acids that signal skin cells to produce more ... The Different Oligopeptides For Every Skin Type. Ices Secret skincare primarily uses six types of oligopeptides that play an ...
Oligopeptide repairs damaged hair structure for improved hair elasticity and resistance. Natural Betaine, a humectant found in ... Derma Healths Skinlabs Oligopeptide Repairing Shampoo is specially formulated for sensitive scalp and weakened hair using ... Home / Personal Care / SkinLabs Oligopeptide Shampoo 300ML. View cart "Aiken Medicated Talc 150G" has been added to your cart. ... Oligopeptide repairs damaged hair structure for improved hair elasticity and resistance. Natural Betaine, a humectant found in ...
Discover the incredible advantages of marine oligopeptides in the field of biochemicals and their potential to revolutionize ... The Surprising Benefits of Marine Oligopeptides in Biochemicals-Sunmyan[Collagen peptides powder]- ... Benefits of Marine Oligopeptides:. 1. Enhanced Bioactivity: Marine oligopeptides possess exceptional bioactivity, making them ... The Surprising Benefits of Marine Oligopeptides in Biochemicals. The Surprising Benefits of Marine Oligopeptides in ...
MVT-602 is an oligopeptide kisspeptin-1 receptor agonist and an investigational drug candidate for egg maturation in women ... MVT-602, an oligopeptide kisspeptin-1 receptor agonist, has the potential to increase luteinizing hormone (LH), which ... MVT-602 is an oligopeptide kisspeptin-1 receptor agonist and an investigational drug candidate for multiple indications and ...
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... oligopeptide-1, snake venom peptide, dipeptide, carnosine, achillea millefolium extract, artemia extract.2 Types for your ... Main ingredients: oligopeptide-1, snake venom peptide, dipeptide, carnosine, achillea millefolium extract, artemia extract.. 2 ... Oligopeptide-1, PEG-75 Bovine Oleoresin glycerides, yarrow (ACHILLEA MILLEFOLIUM) extract, dipeptide diaminobutyrylbenzylamide ...
Collagen TripeptidesMarine collagen peptidesMarine fish oligopeptideTuna peptideOyster PeptidesCorn Protein Peptides ... The companys products include fish collagen peptides, marine fish oligopeptides, sea cucumber peptides, oyster peptides, tuna ... The companys products include fish collagen peptides, marine fish oligopeptides, sea cucumber peptides, oyster peptides, tuna ...
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Photoprocesses in self-assembled complexes of oligopeptides with metalloporphyrins. Mohamed Aoudia, Michael A.J. Rodgers*. * ... Aoudia, M., & Rodgers, M. A. J. (1997). Photoprocesses in self-assembled complexes of oligopeptides with metalloporphyrins. ... Aoudia, M & Rodgers, MAJ 1997, Photoprocesses in self-assembled complexes of oligopeptides with metalloporphyrins, Journal of ... Photoprocesses in self-assembled complexes of oligopeptides with metalloporphyrins. Journal of the American Chemical Society. ...
  • Oligopeptide classes are produced by nonribosomal peptides synthases (NRPS), except cyclamides and microviridins are synthesized through ribosomic pathways. (
  • Examples of oligopeptides include: Amanitins - Cyclic peptides taken from carpophores of several different mushroom species. (
  • This month's survey of recent patent and literature research describes money-making ideas in the personal care industry, ranging from oligopeptides for sensory properties and peptides for hair, to a dandruff treatment and colorless carotenoids for sun damage protection. (
  • After this move, a wide range of high-quality extracted peptides, including hydrolyzed protein peptides, fish collagen peptides, marine fish oligopeptides, oyster peptides, sea cucumber peptides, pea peptides, soy peptides, and walnut peptides can be easily obtained from Alfa Chemistry. (
  • As a result of the different chemical profiles among coexisting strains, the phenology of individual chemotypes dynamically affects the properties of the whole-population with regard to normal oligopeptide material [19], including hepatotoxic peptides like microcystins. (
  • Saccharomyces cerevisiae contains different peptide transporters: Ptr2 and Dal5, specific to di- and tri-peptides, whereas the Oligopeptide transport (OPT) family members import tetra- and pentapeptides (1). (
  • Oligopeptide-34 - a synthetically manufactured peptide containing 13 amino acids (including arginine). (
  • On the other hand, a scrambled peptide, which had the same amino acid composition as and had an amino acid sequence different from the 17-mer oligopeptide, did not respond to any nucleotides. (
  • Furthermore, Fungal Oligopeptide Transporters (FOT) are a novel family of oligopeptide transporters found in fungi. (
  • Oligopeptides are short sequences of amino acids that signal skin cells to produce more collagen and elastin. (
  • Oligopeptide - 1 supports cell growth and activity in order to reinvigorate collagen fibers which makes it advisable for aging skin. (
  • Oligopeptide - 2 regulates collagen production, increases cell proliferation, and facilitates wound healing for those with acne-prone and pigmented skin. (
  • Oligopeptide - 5 is excellent for thinning skin as it aids in cell metabolism to fortify the function of collagen. (
  • The results showed that mice treated with small-molecule oligopeptides exhibited increased vascularization, collagen deposition, and epithelialization, as well as reduced levels of inflammatory markers and oxidative stress. (
  • 4. Nutritional Benefits: Marine oligopeptides are an excellent source of essential amino acids and other vital nutrients. (
  • Active pancreatic enzymes hydrolyze proteins into oligopeptides, which are absorbed directly or hydrolyzed into amino acids. (
  • Oligopeptide-34 decreases melanin synthesis and tyrosinase enzyme activity in melanocytes, decreasing the transfer of melanosomes to new keratinoycte cells. (
  • The conclusion was that 'combination of DAB serum at night and DAB/TGF-β1 biomimetic oligopeptide-68/sunscreen cream in the morning and at noon was effective and safe for facial melasma . (
  • Oligopeptide miracle repair serum mask. (
  • Proton-dependent oligopeptide transporters (POTs) are recognized for their substrate promiscuity due to their ability to transport a wide range of substrates. (
  • Ice's Secret infuses oligopeptides into their basic and advanced serums through freeze-drying technology to stabilize and preserve its potency for fast and promising results. (
  • Ice's Secret skincare primarily uses six types of oligopeptides that play an important role in unlocking the skin's self-repairing abilities. (
  • At Ice's Secret skincare , we have oligopeptide masks for every skin type! (
  • Regarding skincare, oligopeptides are prized ingredients you do not want to miss out on. (
  • Derma Health's Skinlabs Oligopeptide Repairing Shampoo is specially formulated for sensitive scalp and weakened hair using naturally derived ingredients. (
  • This luxurious set includes both the Small Bubble Cleansing Essence and the Bubble Clean Gel, both enriched with nourishing oligopeptide ingredients to give you the ultimate skincare experience. (
  • The antioxidant capabilities of two oligopeptides from sea cucumber intestines, Val-Gly-Thr-Val-Glu-Met and Val-Thr-Pro-Tyr, were determined using ESR spectroscopy to assess their ability to combat hydroxyl radicals, superoxide radicals, and DPPH radicals. (
  • These findings suggest that the oligopeptides from sea cucumber intestines have antioxidant potential, warranting further exploration for their application value. (
  • A series of experiments, including normobaric and hypobaric experiments, examined the effects of sea cucumber oligopeptides, soybean glycopeptides, and their mixtures on mice under hypoxic conditions. (
  • Overall, sea cucumber oligopeptides, soybean glycopeptides, and their combinations all significantly enhanced the tolerance of mice to hypoxia. (
  • Oligopeptides were extracted from sea cucumber intestines using a self-dissolution method, and the optimal extraction conditions, including temperature and pH, were determined using response surface methodology. (
  • These results suggest that oligopeptides extracted from sea cucumber intestines have potential applications in the preparation of functional foods. (
  • The effect of small-molecule oligopeptides extracted from sea cucumber on wound healing in diabetic mice was investigated. (
  • These findings suggest that the use of small-molecule oligopeptides from sea cucumber can significantly promote wound healing in diabetic mice. (
  • Additionally, holothurian oligopeptides play a crucial role in the field of immunology, enhancing immune function, regulating T lymphocyte and NK cell activity. (
  • Combined use of two formulations containing diacetyl boldine, TGF‐β1 biomimetic oligopeptide‐68 with other hypopigmenting/exfoliating agents and sunscreen provides effective and convenient treatment for facial melasma. (
  • The Au disk electrode, which was modified with the designed 17-mer oligopeptide, responded to cyclic AMP but virtually did not respond to any other cyclic nucleotides using the ion channel sensor mechanism. (
  • Netropsin - A basic oligopeptide isolated from Streptomyces netropsis. (
  • Oligopeptide antibiotics from Streptomyces distallicus. (
  • Overall , if you are into skin-lightening or fading pigmentation spots, Oligopeptide-68 might be something to try. (
  • Our company always leads the trend with first-class quality, and makes unremitting efforts to build the first brand of Lowest Price Anti-Wrinkle Oligopeptide-1 Powder. (
  • Using oligopeptide freeze-dried powder preserves the freshness of skincare products at room temperature while preventing an inflammation response for sensitive-skinned individuals. (
  • Oligopeptide repairs damaged hair structure for improved hair elasticity and resistance. (
  • The core oligopeptide-1 component helps to even out skin tone and brighten your complexion, while the dense foam works to cleanse pores, remove dirt and oil, and smooth out the skin's surface. (
  • Holothurian oligopeptide products are obtained through natural extraction, using proteases to hydrolyze fresh sea cucumbers, resulting in holothurian oligopeptides. (
  • Incorporating marine oligopeptides into skincare products can lead to healthier and more youthful-looking skin. (
  • Marine oligopeptides have emerged as a fascinating subject in the world of biochemicals. (
  • In this article, we will explore the captivating world of marine oligopeptides and shed light on their potential to transform the field of biochemicals with their remarkable benefits. (
  • 1. Enhanced Bioactivity: Marine oligopeptides possess exceptional bioactivity, making them suitable for various biological applications. (
  • 2. Promotes Skin Health: Marine oligopeptides have been extensively studied for their beneficial effects on skin health. (
  • 3. Potential Anti-Cancer Properties: Studies have shown that certain marine oligopeptides exhibit anti-cancer activity. (
  • 5. Environmentally Friendly: Marine oligopeptides are derived from sustainable sources such as marine organisms and seaweeds. (
  • 1. Pharmaceutical Industry: Marine oligopeptides hold immense potential in drug discovery and development. (
  • 2. Cosmetics and Skincare: The incorporation of marine oligopeptides into cosmetic formulations has gained traction in recent years. (
  • 3. Agriculture and Aquaculture: Marine oligopeptides have shown promise in enhancing crop growth, improving plant tolerance to stress, and increasing yields. (
  • In conclusion, marine oligopeptides have the potential to revolutionize the field of biochemicals with their remarkable benefits and diverse applications. (
  • By harnessing the power of marine oligopeptides, researchers and professionals can unlock new frontiers in biochemistry and contribute to the development of innovative solutions for a healthier future. (
  • Marine fish oligopeptide--Nanotide (Yangjiang) Biotechnology Co., Ltd. (
  • Marine fish oligopeptides with molecular weights of less than 1 kDa are extracted from cod fish and can be used in food, health care, cosmetics industries, etc. (
  • This acne toner with a variety of oligopeptides and plant extracts is gentle and non-irritating, and it can be absorbed quickly. (
  • Oligopeptide - 6 acts as an antioxidant that evens out skin texture for people with enlarged pores and scarred skin. (
  • Under these optimized conditions, four main oligopeptide fractions were isolated, with fraction IV exhibiting potent antioxidant and DNA-protective properties. (
  • The synthetic modified oligopeptides, available in quantity, served both as immunogens and as chemical standards for quantitative ELISA. (
  • Factory direct supply oligopeptide repair stock skin care product set moisturizing and hydrating repair skin oligopeptide essence oem_Guangzhou Mingyu Cosmetics Manufacturing Co., Ltd. (
  • Oligopeptides infused in pore-minimizing products can lessen the occurrence of breakouts. (
  • Molecular Mechanism of Lotus Seedpod Oligomeric Procyanidins Inhibiting the Absorption of Oligopeptide-Advanced Glycation End Products. (
  • The results showed that both oligopeptides exhibited concentration-dependent free radical scavenging abilities, with Val-Gly-Thr-Val-Glu-Met showing significantly higher efficacy than Val-Thr-Pro-Tyr. (
  • Pepstatins - N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin. (
  • Basically, oligopeptides keep you looking young and fresh as it lessens the appearance of fine lines, wrinkles, and dark spots. (
  • In the S. cerevisiae commercial wine strain EC1118, Fot1 and Fot2 are responsible for a broader range of oligopeptide utilization, which leads to a better fermentation efficiency and cell viability and the production of positive organoleptic compounds in wine when compared to the Fot-knockout strain counterparts (2, 3). (
  • Oligopeptide (OLP)-AGEs, as the main form after digestion , will damage human health once absorbed. (
  • Transform your skincare routine today with the power of oligopeptide technology. (
  • Seebio Holothurian oligopeptides have a wide range of potential applications in multiple industries. (
  • Oligopeptide - 4 enables aging skin to generate new skin cells and increases elastin to fend off wrinkles and infection. (
  • An oligopeptide screened with microfluidic chip-based technique was demonstrated to have high affinity to ovarian cancer cells and demonstrated relatively low binding to other cancer cells, indicating a high specificity. (
  • Therefore, the screened oligopeptide could be used to isolate ovarian cancer cells in a rapid manner, thus greatly expediting the diagnosis and its application as oligopeptide targeting agent for theranostics of this cancer. (
  • As for research, we found one study from 2016 that combined Oligopeptide-68 with sunscreen and another skin-lightening active called Diacetyl Boldine (DAB). (
  • Mass spectrometry analysis identified specific oligopeptides responsible for these protective effects, including two tetrapeptides and one hexapeptide. (
  • For instance, applying a facial mask enriched with oligopeptides allows your skin to remain plump while fighting the effects of UV damage. (