Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. In animals they are found on mucosal surfaces, within phagocytic granules, and on the surface of the body. They are also found in insects and plants. Among others, this group includes the DEFENSINS, protegrins, tachyplesins, and thionins. They displace DIVALENT CATIONS from phosphate groups of MEMBRANE LIPIDS leading to disruption of the membrane.
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 class of antimicrobial peptides discovered in the skin of XENOPUS LAEVIS. They kill bacteria by permeabilizing cell membranes without exhibiting significant toxicity against mammalian cells.
A mixture of polymyxins B1 and B2, obtained from Bacillus polymyxa strains. They are basic polypeptides of about eight amino acids and have cationic detergent action on cell membranes. Polymyxin B is used for infections with gram-negative organisms, but may be neurotoxic and nephrotoxic.
Substances that reduce the growth or reproduction of BACTERIA.
Family of antimicrobial peptides that have been identified in humans, animals, and plants. They are thought to play a role in host defenses against infections, inflammation, wound repair, and acquired immunity.
Substances that prevent infectious agents or organisms from spreading or kill infectious agents in order to prevent the spread of infection.
Positively charged atoms, radicals or groups of atoms which travel to the cathode or negative pole during electrolysis.
Any tests that demonstrate the relative efficacy of different chemotherapeutic agents against specific microorganisms (i.e., bacteria, fungi, viruses).
DEFENSINS found mainly in epithelial cells.
A group of small, histidine-rich, cationic peptides in human SALIVA which are antibacterial and antifungal.

Range of activity and metabolic stability of synthetic antibacterial glycopeptides from insects. (1/2987)

Antibacterial glycopeptides isolated from insects are exciting bio-oligomers because they represent a family of compounds in which the structural and functional effects of incorporating short O-linked sugars to protein fragments can be studied. Additionally, their high activity in vitro warrants detailed further drug development efforts. Due to the limited availability of the isolated material, we used synthetic glycopeptides and some analogs to investigate the range of activity of drosocin and pyrrhocoricin. While addition of the Gal-GalNAc disaccharide to the natural mid-chain position generally increased the antibacterial activity of drosocin, pyrrhocoricin lacking sugar appeared to be more potent, with an IC50 against Escherichia coli D22 of 150 nM. Although glycosylated drosocin was active against E. coli in the low microM range in vitro, this peptide was completely inactive when injected into mice. The lack of in vivo activity of drosocin could be explained by the unusually high degradation rate of the peptides in mammalian sera. The early degradation products were inactive in vitro. In contrast, the peptides were considerably more stable in insect hemolymph, where their natural activity is manifested.  (+info)

Biological properties of structurally related alpha-helical cationic antimicrobial peptides. (2/2987)

A series of alpha-helical cationic antimicrobial peptide variants with small amino acid changes was designed. Alterations in the charge, hydrophobicity, or length of the variant peptides did not improve the antimicrobial activity, and there was no statistically significant correlation between any of these factors and the MIC for Pseudomonas aeruginosa, Escherichia coli, or Salmonella typhimurium. Individual peptides demonstrated synergy with conventional antibiotics against antibiotic-resistant strains of P. aeruginosa. The peptides varied considerably in the ability to bind E. coli O111:B4 lipopolysaccharide (LPS), and this correlated significantly with their antimicrobial activity and ability to block LPS-stimulated tumor necrosis factor and interleukin-6 production. In general, the peptides studied here demonstrated a broad range of activities, including antimicrobial, antiendotoxin, and enhancer activities.  (+info)

Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins, protegrins, and other antimicrobial peptides. (3/2987)

Positively charged antimicrobial peptides with membrane-damaging activity are produced by animals and humans as components of their innate immunity against bacterial infections and also by many bacteria to inhibit competing microorganisms. Staphylococcus aureus and Staphylococcus xylosus, which tolerate high concentrations of several antimicrobial peptides, were mutagenized to identify genes responsible for this insensitivity. Several mutants with increased sensitivity were obtained, which exhibited an altered structure of teichoic acids, major components of the Gram-positive cell wall. The mutant teichoic acids lacked D-alanine, as a result of which the cells carried an increased negative surface charge. The mutant cells bound fewer anionic, but more positively charged proteins. They were sensitive to human defensin HNP1-3, animal-derived protegrins, tachyplesins, and magainin II, and to the bacteria-derived peptides gallidermin and nisin. The mutated genes shared sequence similarity with the dlt genes involved in the transfer of D-alanine into teichoic acids from other Gram-positive bacteria. Wild-type strains bearing additional copies of the dlt operon produced teichoic acids with higher amounts of D-alanine esters, bound cationic proteins less effectively and were less sensitive to antimicrobial peptides. We propose a role of the D-alanine-esterified teichoic acids which occur in many pathogenic bacteria in the protection against human and animal defense systems.  (+info)

Recombinant bactericidal/permeability-increasing protein (rBPI21) in combination with sulfadiazine is active against Toxoplasma gondii. (4/2987)

The activity of recombinant bactericidal/permeability-increasing protein (rBPI21), alone or in combination with sulfadiazine, on the intracellular replication of Toxoplasma gondii was assessed in vitro and in mice with acute toxoplasmosis. rBPI21 markedly inhibited the intracellular growth of T. gondii in human foreskin fibroblasts (HFFs). Following 72 h of exposure, the 50% inhibitory concentration of rBPI21 for T. gondii was 2.6 micrograms/ml, whereas only slight cytotoxicity for HFF cells was observed at the concentrations tested. Subsequent mathematical analyses revealed that the combination of rBPI21 with sulfadiazine yielded slight to moderate synergistic effects against T. gondii in vitro. Infection of mice orally with C56 cysts or intraperitoneally (i.p.) with RH tachyzoites resulted in 100% mortality, whereas prolongation of the time to death or significant survival (P = 0.002) was noted for those animals treated with 5 to 20 mg of rBPI21 per kg of body weight per day. Treatment with rBPI21 in combination with sulfadiazine resulted in significant (P = 0.0001) survival of mice infected i.p. with tachyzoites but not of mice infected orally with T. gondii cysts. These results indicate that rBPI21 is active in vitro and in vivo against T. gondii and that its activity is significantly enhanced when it is used in combination with sulfadiazine. To our knowledge, this is the first report of the activity of rBPI21 against a protozoan parasite.  (+info)

In vitro antibacterial properties of pexiganan, an analog of magainin. (5/2987)

Pexiganan, a 22-amino-acid antimicrobial peptide, is an analog of the magainin peptides isolated from the skin of the African clawed frog. Pexiganan exhibited in vitro broad-spectrum antibacterial activity when it was tested against 3,109 clinical isolates of gram-positive and gram-negative, anaerobic and aerobic bacteria. The pexiganan MIC at which 90% of isolates are inhibited (MIC90) was 32 micrograms/ml or less for Staphylococcus spp., Streptococcus spp., Enterococcus faecium, Corynebacterium spp., Pseudomonas spp., Acinetobacter spp., Stenotrophomonas spp., certain species of the family Enterobacteriaceae, Bacteroides spp., Peptostreptococcus spp., and Propionibacterium spp. Comparison of the MICs and minimum bactericidal concentrations (MBCs) of pexiganan for 143 isolates representing 32 species demonstrated that for 92% of the isolates tested, MBCs were the same or within 1 twofold difference of the MICs, consistent with a bactericidal mechanism of action. Killing curve analysis showed that pexiganan killed Pseudomonas aeruginosa rapidly, with 10(6) organisms/ml eliminated within 20 min of treatment with 16 micrograms of pexiganan per ml. No evidence of cross-resistance to a number of other antibiotic classes was observed, as determined by the equivalence of the MIC50s and the MIC90s of pexiganan for strains resistant to oxacillin, cefazolin, cefoxitin, imipenem, ofloxacin, ciprofloxacin, gentamicin, and clindamicin versus those for strains susceptible to these antimicrobial agents. Attempts to generate resistance in several bacterial species through repeated passage with subinhibitory concentrations of pexiganan were unsuccessful. In conclusion, pexiganan exhibits properties in vitro which make it an attractive candidate for development as a topical antimicrobial agent.  (+info)

A gene encoding a hevein-like protein from elderberry fruits is homologous to PR-4 and class V chitinase genes. (6/2987)

We isolated SN-HLPf (Sambucus nigra hevein-like fruit protein), a hevein-like chitin-binding protein, from mature elderberry fruits. Cloning of the corresponding gene demonstrated that SN-HLPf is synthesized as a chimeric precursor consisting of an N-terminal chitin-binding domain corresponding to the mature elderberry protein and an unrelated C-terminal domain. Sequence comparisons indicated that the N-terminal domain of this precursor has high sequence similarity with the N-terminal domain of class I PR-4 (pathogenesis-related) proteins, whereas the C terminus is most closely related to that of class V chitinases. On the basis of these sequence homologies the gene encoding SN-HLPf can be considered a hybrid between a PR-4 and a class V chitinase gene.  (+info)

Endocytosis of heparin-binding protein (CAP37) is essential for the enhancement of lipopolysaccharide-induced TNF-alpha production in human monocytes. (7/2987)

Heparin-binding protein (HBP), also known as CAP37, is a proteolytically inactive serine protease homologue that is released from activated granulocytes. However, HBP is not a biologically inactive molecule but rather a multifunctional protein with properties that include the enhancement of LPS-induced TNF-alpha production from monocytes. We have previously demonstrated that HBP is internalized in monocytes. In the current study, we hypothesize that HBP is internalized in monocytes via endocytosis, and this internalization is an important mechanism by which HBP enhances LPS-induced TNF-alpha release. Using whole blood from healthy donors and flow cytometry, we found that colchicine (0.1-10 mM), cytochalasin D (1000 microM), NH4Cl (10-50 mM), and bafilomycin A1 (0.1-3 microM) significantly reduced the affinity of FITC-HBP for CD14-positive monocytes. Using isolated human monocytes and ELISA, we found that colchicine (0.1 mM), cytochalasin D (30 and 300 microM), NH4Cl (30 mM), and bafilomycin A1 (1 microM) significantly reduced the effect of HBP (10 microg/ml) to enhance LPS (10 ng/ml)-induced TNF-alpha release after 24 h. These findings demonstrate that internalization of HBP in monocytes is essential for the enhancement of LPS-induced TNF-alpha release. Transport of HBP to an activating compartment depends on intact F-actin polymerization and endosomal acidification, an important mechanism for endosomal protein sorting and trafficking.  (+info)

Transfer of a cathelicidin peptide antibiotic gene restores bacterial killing in a cystic fibrosis xenograft model. (8/2987)

Recent studies suggest that the gene defect in cystic fibrosis (CF) leads to a breach in innate immunity. We describe a novel genetic strategy for reversing the CF-specific defect of antimicrobial activity by transferring a gene encoding a secreted cathelicidin peptide antibiotic into the airway epithelium grown in a human bronchial xenograft model. The airway surface fluid (ASF) from CF xenografts failed to kill Pseudomonas aeruginosa or Staphylococcus aureus. Partial reconstitution of CF transmembrane conductance regulator expression after adenovirus-mediated gene transfer restored the antimicrobial activity of ASF from CF xenografts to normal levels. Exposure of CF xenografts to an adenovirus expressing the human cathelicidin LL-37/hCAP-18 increased levels of this peptide in the ASF three- to fourfold above the normal concentrations, which were equivalent in ASF from CF and normal xenografts before gene transfer. The increase of LL-37 was sufficient to restore bacterial killing to normal levels. The data presented describe an alternative genetic approach to the treatment of CF based on enhanced expression of an endogenous antimicrobial peptide and provide strong evidence that expression of antimicrobial peptides indeed protects against bacterial infection.  (+info)

Antimicrobial cationic peptides (ACPs) are a group of small, naturally occurring peptides that possess broad-spectrum antimicrobial activity against various microorganisms, including bacteria, fungi, viruses, and parasites. They are called "cationic" because they contain positively charged amino acid residues (such as lysine and arginine), which allow them to interact with and disrupt the negatively charged membranes of microbial cells.

ACPs are produced by a wide range of organisms, including humans, animals, and plants, as part of their innate immune response to infection. They play an important role in protecting the host from invading pathogens by directly killing them or inhibiting their growth.

The antimicrobial activity of ACPs is thought to be mediated by their ability to disrupt the membranes of microbial cells, leading to leakage of cellular contents and death. Some ACPs may also have intracellular targets, such as DNA or protein synthesis, that contribute to their antimicrobial activity.

ACPs are being studied for their potential use as therapeutic agents to treat infectious diseases, particularly those caused by drug-resistant bacteria. However, their clinical application is still in the early stages of development due to concerns about their potential toxicity to host cells and the emergence of resistance mechanisms in microbial pathogens.

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.

Magainins are a group of antimicrobial peptides that were first isolated from the skin of the African clawed frog, Xenopus laevis. These peptides have broad-spectrum activity against various microorganisms including bacteria, fungi, and enveloped viruses. Magainins are thought to play a crucial role in the innate immune system of the frog, helping to protect the animal from infection through its skin. They function by disrupting the membranes of microbial cells, leading to cell death. Magainins have been studied for their potential use as therapeutic agents, particularly in the context of antibiotic-resistant bacterial infections. However, more research is needed to fully understand their mechanisms of action and safety profile before they can be widely used in clinical settings.

Polymyxin B is an antibiotic derived from the bacterium Paenibacillus polymyxa. It belongs to the class of polypeptide antibiotics and has a cyclic structure with a hydrophobic and a hydrophilic region, which allows it to interact with and disrupt the bacterial cell membrane. Polymyxin B is primarily active against gram-negative bacteria, including many multidrug-resistant strains. It is used clinically to treat serious infections caused by these organisms, such as sepsis, pneumonia, and urinary tract infections. However, its use is limited due to potential nephrotoxicity and neurotoxicity.

Anti-bacterial agents, also known as antibiotics, are a type of medication used to treat infections caused by bacteria. These agents work by either killing the bacteria or inhibiting their growth and reproduction. There are several different classes of anti-bacterial agents, including penicillins, cephalosporins, fluoroquinolones, macrolides, and tetracyclines, among others. Each class of antibiotic has a specific mechanism of action and is used to treat certain types of bacterial infections. It's important to note that anti-bacterial agents are not effective against viral infections, such as the common cold or flu. Misuse and overuse of antibiotics can lead to antibiotic resistance, which is a significant global health concern.

Defensins are small, cationic host defense peptides that contribute to the innate immune system's response against microbial pathogens. They are produced by various cell types, including neutrophils, epithelial cells, and some bone marrow-derived cells. Defensins have a broad spectrum of antimicrobial activity against bacteria, fungi, viruses, and enveloped lipid bilayers.

Defensins are classified into two main groups: α-defensins and β-defensins. Human α-defensins include human neutrophil peptides (HNP) 1-4 and human defensin 5, 6 (HD5, HD6). These are primarily produced by neutrophils and Paneth cells in the small intestine. β-defensins, on the other hand, are produced by various epithelial cells throughout the body.

Defensins work by disrupting the microbial membrane's integrity, leading to cell lysis and death. They also have immunomodulatory functions, such as chemotaxis of immune cells, modulation of cytokine production, and enhancement of adaptive immune responses. Dysregulation of defensin expression has been implicated in several diseases, including inflammatory bowel disease, chronic obstructive pulmonary disease, and certain skin disorders.

Anti-infective agents are a class of medications that are used to treat infections caused by various microorganisms such as bacteria, viruses, fungi, and parasites. These agents work by either killing the microorganism or inhibiting its growth, thereby helping to control the infection and alleviate symptoms.

There are several types of anti-infective agents, including:

1. Antibiotics: These are medications that are used to treat bacterial infections. They work by either killing bacteria (bactericidal) or inhibiting their growth (bacteriostatic).
2. Antivirals: These are medications that are used to treat viral infections. They work by interfering with the replication of the virus, preventing it from spreading and causing further damage.
3. Antifungals: These are medications that are used to treat fungal infections. They work by disrupting the cell membrane of the fungus, killing it or inhibiting its growth.
4. Antiparasitics: These are medications that are used to treat parasitic infections. They work by either killing the parasite or inhibiting its growth and reproduction.

It is important to note that anti-infective agents are not effective against all types of infections, and it is essential to use them appropriately to avoid the development of drug-resistant strains of microorganisms.

A cation is a type of ion, which is a charged particle, that has a positive charge. In chemistry and biology, cations are formed when a neutral atom loses one or more electrons during chemical reactions. The removal of electrons results in the atom having more protons than electrons, giving it a net positive charge.

Cations are important in many biological processes, including nerve impulse transmission, muscle contraction, and enzyme function. For example, sodium (Na+), potassium (K+), calcium (Ca2+), and magnesium (Mg2+) are all essential cations that play critical roles in various physiological functions.

In medical contexts, cations can also be relevant in the diagnosis and treatment of various conditions. For instance, abnormal levels of certain cations, such as potassium or calcium, can indicate specific diseases or disorders. Additionally, medications used to treat various conditions may work by altering cation concentrations or activity within the body.

Microbial sensitivity tests, also known as antibiotic susceptibility tests (ASTs) or bacterial susceptibility tests, are laboratory procedures used to determine the effectiveness of various antimicrobial agents against specific microorganisms isolated from a patient's infection. These tests help healthcare providers identify which antibiotics will be most effective in treating an infection and which ones should be avoided due to resistance. The results of these tests can guide appropriate antibiotic therapy, minimize the potential for antibiotic resistance, improve clinical outcomes, and reduce unnecessary side effects or toxicity from ineffective antimicrobials.

There are several methods for performing microbial sensitivity tests, including:

1. Disk diffusion method (Kirby-Bauer test): A standardized paper disk containing a predetermined amount of an antibiotic is placed on an agar plate that has been inoculated with the isolated microorganism. After incubation, the zone of inhibition around the disk is measured to determine the susceptibility or resistance of the organism to that particular antibiotic.
2. Broth dilution method: A series of tubes or wells containing decreasing concentrations of an antimicrobial agent are inoculated with a standardized microbial suspension. After incubation, the minimum inhibitory concentration (MIC) is determined by observing the lowest concentration of the antibiotic that prevents visible growth of the organism.
3. Automated systems: These use sophisticated technology to perform both disk diffusion and broth dilution methods automatically, providing rapid and accurate results for a wide range of microorganisms and antimicrobial agents.

The interpretation of microbial sensitivity test results should be done cautiously, considering factors such as the site of infection, pharmacokinetics and pharmacodynamics of the antibiotic, potential toxicity, and local resistance patterns. Regular monitoring of susceptibility patterns and ongoing antimicrobial stewardship programs are essential to ensure optimal use of these tests and to minimize the development of antibiotic resistance.

Beta-defensins are a group of small, cationic host defense peptides that play an important role in the innate immune system. They have broad-spectrum antimicrobial activity against various pathogens, including bacteria, fungi, and viruses. Beta-defensins are produced by epithelial cells, phagocytes, and other cell types in response to infection or inflammation. They function by disrupting the membranes of microbes, leading to their death. Additionally, beta-defensins can also modulate the immune response by recruiting immune cells to the site of infection and regulating inflammation. Mutations in beta-defensin genes have been associated with increased susceptibility to infectious diseases.

Histatins are a group of histidine-rich proteins that are produced by the salivary glands in humans and other mammals. They have various functions, including antibacterial, antifungal, and wound healing properties. Histatins are composed of 21-24 amino acids and are named based on their molecular weight. The most well-studied histatins are Histatin 1, Histatin 3, and Histatin 5. They play a crucial role in maintaining oral health by helping to prevent dental caries and oral candidiasis.

As these peptides still keep the ability to form complexes with DNA molecules with no prejudice to their ability to bind to ... Aiming to identify the features necessary for the antifungal activity of crotamine, two linear short peptides, each comprising ... We previously demonstrated that crotamine derived short linear peptides were not very effective as antifungal, although the non ... Interestingly, the presence of cysteine residues in the structure of these linear peptides highly influenced the antifungal ...
title = "Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents",. abstract = "Antimicrobial peptides (AMPs ... Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents. In: Biomaterials. 2011 ; Vol. 32, No. 8. pp. 2204- ... Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents. Nikken Wiradharma, Ulung Khoe, Charlotte A.E. Hauser ... Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents. Biomaterials. 2011 Mar;32(8):2204-2212. doi: 10.1016 ...
Polymyxins and other cationic antimicrobial peptides attach to the LPS cell walls of bacteria by virtue of the highly ... "Bacterial resistance to cationic antimicrobial peptides". Critical Reviews in Microbiology. 39 (2): 180-195. doi:10.3109/ ... The PhoPQ system, which detects similar situations and the presence of antimicrobial peptides, can also cross-trigger PmrA via ... The modifications also provide cross-resistance to host immunity factors, specifically antimicrobial peptides and lysozyme. EC ...
LPS Interaction with Antimicrobial Peptides (AMPs)-The First Line of Defense in Innate Immunity. Cationic antimicrobial ... Abdelbaqi, S.; Deslouches, B.; Steckbeck, J.; Montelaro, R.; Reed, D.S. Novel engineered cationic antimicrobial peptides ... pestis to cationic antimicrobial peptides by a decrease in their affinity for the LPS, may promote the growth of Y. pestis in ... and antimicrobial cationic peptide resistance, the Y. pestis version of this complex macromolecule should include in its core ...
Cationic antimicrobial peptides (CAMPs) represent one of the most effective components of the host innate immune response. Here ... Cationic antimicrobial peptides (CAMPs) represent one of the most effective components of the host innate immune response. Here ... Inactivation of the gene encoding the cationic antimicrobial peptide resistance factor MprF increases biofilm formation but ... Broad-spectrum antimicrobial peptide resistance by MprF-mediated aminoacylation and flipping of phospholipids. ...
GO loaded with cationic antimicrobial peptide AWRK6 exerts a rosy neutralization effect on endotoxin activity, with no obvious ... Efficacy of graphene oxide-loaded cationic antimicrobial peptide AWRK6 on the neutralization of endotoxin activity and in the ... Efficacy of graphene oxide-loaded cationic antimicrobial peptide AWRK6 on the neutralization of endotoxin activity and in the ... Conclusion: GO loaded with cationic antimicrobial peptide AWRK6 exerts a rosy neutralization effect on endotoxin activity, with ...
Peschel, A., and Sahl, H.-G. (2006). The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. ... 2016). Interleukin-17A (IL-17A) and IL-17F are critical for antimicrobial peptide production and clearance of Staphylococcus ... Burgey, C., Kern, W. V., Römer, W., and Rieg, S. (2016). Differential induction of innate defense antimicrobial peptides in ... Interleukin-22 regulates antimicrobial peptide expression and keratinocyte differentiation to control Staphylococcus aureus ...
Categories: Antimicrobial Cationic Peptides Image Types: Photo, Illustrations, Video, Color, Black&White, PublicDomain, ...
Antimicrobial peptides (AMPs) seem to meet these expectations. AMPs are produced by bacteria, viruses, plants, and animals, and ... The emergence of resistance in microorganisms on a global scale has made it necessary to search for new antimicrobial factors. ... Cationic antimicrobial peptides: towards clinical applications. Expert Opin Investig Drugs. 2000; 9(8): 1723-1729. ... Antimicrobial peptides may be applied topically and systemically. Among the peptides used topically, a very important area for ...
In turn, pancreatic factors, such as the excretion of antimicrobials, might have a substantial impact on the composition and ... The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. Rev. Microbiol. 4:529-36 ... The co-evolution of host cationic antimicrobial peptides and microbial resistance. Nat. Rev. Microbiol. 4:529-36 ... Cathelicidin-related antimicrobial peptide modulates the severity of acute pancreatitis in mice. Mol. Med. Rep. 13:3881-85 ...
These drug candidates are cationic amphiphiles, small α-helical peptides that have an affinity for both water and lipids. They ... They have shown promise as antimicrobials and anticancer drugs, but they are costly to manufacture. Worse, they are quickly ... Instead of traditional peptides, it creates peptide mimics-asymmetric triplex metallohelices. These structures, which have a ... While cationic amphiphiles have attracted research interest, they have been a source of frustration, too, for not only are they ...
... and antimicrobial agents. Multidisciplinary approaches are required across health care settings as well as environment and ... The crisis of antimicrobial resistance has been ascribed to the misuse of these agents and due to unavailability of newer drugs ... Cationic host defense (antimicrobial) peptides. Curr Opin Immunol. 2006;18(1):24-30. ... Antimicrobial peptides (AMPs) are emerging antimicrobial agents found in animals, microorganisms, and plants and have a broader ...
Drug resistance: antimicrobial 01501 beta-Lactam resistance. 01502 Vancomycin resistance. 01503 Cationic antimicrobial peptide ... 01054 Nonribosomal peptide structures. 01053 Biosynthesis of siderophore group nonribosomal peptides. 01055 Biosynthesis of ...
Hispidalin / Cationic Bioactive Peptide / Antimicrobial / Antioxidant / Seeds: Study yielded a bioactive peptide, Hispidalin, ... Cationic Bioactive Peptide from the Seeds of Benincasa hispida / Sunayana Sharma, Hirday Narain Verma, and Nilesh Kumar Sharma ... Antimicrobial screening showed activity against test organisms A. aureus and E. coli. Antimicrobial and antioxidant activities ... ANTIMICROBIAL STUDIES ON METHANOL EXTRACT OF BENINCASA HISPIDA COGN., FRUIT / D. Natarajan, R.J. Lavarasan, S. Chandra babu, M. ...
Lipid Membrane Interactions of the Cationic Antimicrobial Peptide Chimeras Melimine and Cys-Melimine. Berry, T., Dutta, D., ... Antimicrobial activity of immobilized lactoferrin and lactoferricin. Chen, R., Cole, N., Dutta, D., Kumar, N. & Willcox, M. D. ... Esculentin-1a derived peptides kill Pseudomonas aeruginosa biofilm on soft contact lenses and retain antibacterial activity ... Activity of a melimine derived peptide Mel4 against Stenotrophomonas, Delftia, Elizabethkingia, Burkholderia and ...
2014): Small cationic antimicrobial peptides delocalize peripheral membrane proteins, Proceedings of the National Academy of ... and her team have been studying the MP196 peptide as a representative of a group of very small positively charged peptides that ... Small peptides attack bacteria in many different ways and may well become a new generation of antibiotics. Biologists at the ... Together with colleagues from Germany, Austria and Canada, she reports on the peptides mode of action in the journal ...
Antimicrobial peptides MBI 226, currently known as omiganan pentahydrochloride, is a topical cationic peptide derived from the ... et al. Antimicrobial activity of de novo designed cationic peptides against multi-resistant clinical isolates. Eur J Med Chem ... Omiganan pentahydrochloride (MBI 226), a topical 12-amino-acid cationic peptide: Spectrum of antimicrobial activity and ... Antimicrobial activity of de novo designed cationic peptides against multi-resistant clinical isolates. Eur J Med Chem 2014;71: ...
Cationic antimicrobial peptides are a class of small, positively charged peptides known for their broad-spectrum ... Cationic antimicrobial peptides are a class of small, positively charged peptides known for their broad-spectrum ... The polyphemusin family of antimicrobial peptides : activity through structure and membrane interactions Powers, Jon-Paul ... Peptides from the horseshoe crab, the polyphemusins and tachyplesins, are some of the most active peptides isolated from nature ...
Based on this PLS model, a series of cationic antimicrobial peptides (AMPs), with relatively high antimicrobial activity was ... Based on this PLS model, a series of cationic antimicrobial peptides (AMPs), with relatively high antimicrobial activity was ... Descriptors for the Structure-Activity Relationships of Antimicrobial Peptides, Protein & Peptide Letters 2009; 16 (2) . https ... Keywords: Antimicrobial peptides (AMPs), HESH, Genetic algorithm (GA), Partial least square (PLS), Quantitative ...
Reduced cytotoxicity and enhanced bioactivity of cationic antimicrobial peptides liposomes in cell cultures and 3D epidermis ... Computationally designed bispecific MD2/CD14 binding peptides show TLR4 agonist activity. Michaeli, Amit; Mezan, Shaul; ...
Cationic NCRs perform in vitro antimicrobial activities (15, 16) partly by disturbing the integrity of the microbial membranes ... S6). Deposition of extracellular material was also induced by cationic NCRs with a pI below 9, whereas cationic peptides with a ... and cationic peptides in the legumes studied: only G. uralensis lacked cationic NCRs, whereas those species hosting EB ... or cationic NCRs. Except for NCR102, significant biofilm formation was induced by the cationic peptides (Fig. 3E). ...
The activity of the tyrocidine peptide complex (Trc mixture) and purified tyrocidines exhibited minimum inhibition ... Frecer V. ( 2006). QSAR analysis of antimicrobial and haemolytic effects of cyclic cationic antimicrobial peptides derived from ... Analyses of dose-response curves to compare the antimicrobial activity of model cationic α-helical peptides highlights the ... Rydlo T., Miltz J., Mor A. ( 2006). Eukaryotic antimicrobial peptides: promises and premises in food safety. J Food Sci 71:R125 ...
Rationally Modified Antimicrobial Peptides from the N-Terminal Domain of Human RNase 3 Show Exceptional Serum Stability / ... Our previous work identified an antimicrobial region at the N-terminus of the eosinophil cationic protein (ECP). [...] 2022 - ... Antimicrobial proteins and peptides (AMPs) are the key players in host innate immunity. [...] 2019 - 10.3389/fmicb.2019.01357 ... Antimicrobial proteins and peptides offer a multifaceted mechanism suitable to fight bacterial resistance. [...] 2019 - 10.3389 ...
Synthetic cationic antimicrobial peptides bind with their hydrophobic parts to drug site II of human serum albumin. ... Lamprey albumin contains a 23-amino acid putative signal peptide and a 6-residue putative propeptide, which, when cleaved, ...
Furthermore, they start their debridement by releasing highly active antimicrobial substances (cationic peptides and ...
... both the immobilization of cationic peptides onto polymeric surfaces as well as the incorporation of related antimicrobial ... Antimicrobial peptides, a range of naturally occurring and synthetically generated peptide structures, take this even further ... The related peptides consist of 12 to 50 amino acids, including at least two often more cationic amino acids plus hydrophobic ... The combination of amino acids with cationic and hydrophobic side chains was reported to increase the efficacy of the peptide ...
Inactivation of the gene encoding the cationic antimicrobial peptide resistance factor MprF increases biofilm formation but ... Antimicrobials and antimicrobial resistance. Antimicrobial resistance (AMR) is now recognised as one of the major challenges ... Antimicrobial resistance in H pylori is widespread, and although the prevalence of antimicrobial resistance shows regional ... This study highlights the public health importance of enhanced antimicrobial resistance surveillance and strict antimicrobial ...
... develops progressive approaches that enable the loading and local delivery of a unique group of cationic antimicrobial peptides ... Local delivery of antimicrobial peptides from titanium surface for the prevention of implant-associated infections (2013) ... Local delivery of antimicrobial peptides using self-organized TiO2 nanotubes for implant-related infections (2011) ... Among the potential alternatives are the antimicrobial peptides (AMPs). Because of their broad-spectrum bactericidal ability, ...

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