Peptaibols: A group of peptides characterized by length of 1-2 dozen residues with a high proportion of them being non-proteinogenic, notably alpha-aminoisobutyric acid (Aib) and isovaline, and have a C-terminal amino alcohol and N terminal alkyl group. They are found in FUNGI and some are ANTI-INFECTIVE AGENTS. They form channels or pores in target organisms. The term is a contraction of peptide-Aib-alcohol.Lipid Bilayers: Layers of lipid molecules which are two molecules thick. Bilayer systems are frequently studied as models of biological membranes.Ion Channels: Gated, ion-selective glycoproteins that traverse membranes. The stimulus for ION CHANNEL GATING can be due to a variety of stimuli such as LIGANDS, a TRANSMEMBRANE POTENTIAL DIFFERENCE, mechanical deformation or through INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS.Melitten: Basic polypeptide from the venom of the honey bee (Apis mellifera). It contains 26 amino acids, has cytolytic properties, causes contracture of muscle, releases histamine, and disrupts surface tension, probably due to lysis of cell and mitochondrial membranes.Ionophores: Chemical agents that increase the permeability of biological or artificial lipid membranes to specific ions. Most ionophores are relatively small organic molecules that act as mobile carriers within membranes or coalesce to form ion permeable channels across membranes. Many are antibiotics, and many act as uncoupling agents by short-circuiting the proton gradient across mitochondrial membranes.Niclosamide: An antihelmintic that is active against most tapeworms. (From Martindale, The Extra Pharmacopoeia, 30th ed, p48)Phosphatidylcholines: Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a choline moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and choline and 2 moles of fatty acids.Biophysical Phenomena: The physical characteristics and processes of biological systems.Octanes: Eight-carbon saturated hydrocarbon group of the methane series. Include isomers and derivatives.Biophysics: The study of PHYSICAL PHENOMENA and PHYSICAL PROCESSES as applied to living things.Electric Conductivity: The ability of a substrate to allow the passage of ELECTRONS.Tetrathionic Acid: A sulfuric acid dimer, formed by disulfide linkage. This compound has been used to prolong coagulation time and as an antidote in cyanide poisoning.Membranes, Artificial: Artificially produced membranes, such as semipermeable membranes used in artificial kidney dialysis (RENAL DIALYSIS), monomolecular and bimolecular membranes used as models to simulate biological CELL MEMBRANES. These membranes are also used in the process of GUIDED TISSUE REGENERATION.Trichoderma: A mitosporic fungal genus frequently found in soil and on wood. It is sometimes used for controlling pathogenic fungi. Its teleomorph is HYPOCREA.Spin Labels: Molecules which contain an atom or a group of atoms exhibiting an unpaired electron spin that can be detected by electron spin resonance spectroscopy and can be bonded to another molecule. (McGraw-Hill Dictionary of Chemical and Technical Terms, 4th ed)Electrochemistry: The study of chemical changes resulting from electrical action and electrical activity resulting from chemical changes.Anti-Bacterial Agents: Substances that reduce the growth or reproduction of BACTERIA.Protein Structure, Secondary: 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.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Cyclic N-Oxides: Heterocyclic compounds in which an oxygen is attached to a cyclic nitrogen.Phosphatidylethanolamines: Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to an ethanolamine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and ethanolamine and 2 moles of fatty acids.Membrane Potentials: The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization).Dimyristoylphosphatidylcholine: A synthetic phospholipid used in liposomes and lipid bilayers for the study of biological membranes.Membrane Fluidity: The motion of phospholipid molecules within the lipid bilayer, dependent on the classes of phospholipids present, their fatty acid composition and degree of unsaturation of the acyl chains, the cholesterol concentration, and temperature.Glucuronides: Glycosides of GLUCURONIC ACID formed by the reaction of URIDINE DIPHOSPHATE GLUCURONIC ACID with certain endogenous and exogenous substances. Their formation is important for the detoxification of drugs, steroid excretion and BILIRUBIN metabolism to a more water-soluble compound that can be eliminated in the URINE and BILE.Glucuronosyltransferase: A family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines, and fatty acids. They function as drug-metabolizing enzymes that catalyze the conjugation of UDPglucuronic acid to a variety of endogenous and exogenous compounds. EC 2.4.1.17.Amino Acid Sequence: 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.Peptides: 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.Solvents: Liquids that dissolve other substances (solutes), generally solids, without any change in chemical composition, as, water containing sugar. (Grant & Hackh's Chemical Dictionary, 5th ed)Water: A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Mathematics: The deductive study of shape, quantity, and dependence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Molecular Sequence Data: 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.Circular Dichroism: 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)Hydrogen Bonding: A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.Magnetic Resonance Spectroscopy: 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).X-Ray Diffraction: The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Alamethicin: A cyclic nonadecapeptide antibiotic that can act as an ionophore and is produced by strains of Trichoderma viride. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Models, Structural: A representation, generally small in scale, to show the structure, construction, or appearance of something. (From Random House Unabridged Dictionary, 2d ed)Protein Conformation: 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).Electron Spin Resonance Spectroscopy: A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Molecular Conformation: The characteristic three-dimensional shape of a molecule.Thermodynamics: A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)Liposomes: Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins.Computer Simulation: Computer-based representation of physical systems and phenomena such as chemical processes.Static Electricity: The accumulation of an electric charge on a objectPhysicochemical Phenomena: The physical phenomena describing the structure and properties of atoms and molecules, and their reaction and interaction processes.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Chemistry, Physical: The study of CHEMICAL PHENOMENA and processes in terms of the underlying PHYSICAL PHENOMENA and processes.Kinetics: The rate dynamics in chemical or physical systems.Phospholipids: Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.Gramicidin: A group of peptide antibiotics from BACILLUS brevis. Gramicidin C or S is a cyclic, ten-amino acid polypeptide and gramicidins A, B, D are linear. Gramicidin is one of the two principal components of TYROTHRICIN.Methanol: A colorless, flammable liquid used in the manufacture of FORMALDEHYDE and ACETIC ACID, in chemical synthesis, antifreeze, and as a solvent. Ingestion of methanol is toxic and may cause blindness.Potentiometry: Solution titration in which the end point is read from the electrode-potential variations with the concentrations of potential determining ions. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Molecular Probes: A group of atoms or molecules attached to other molecules or cellular structures and used in studying the properties of these molecules and structures. Radioactive DNA or RNA sequences are used in MOLECULAR GENETICS to detect the presence of a complementary sequence by NUCLEIC ACID HYBRIDIZATION.Ions: An atom or group of atoms that have a positive or negative electric charge due to a gain (negative charge) or loss (positive charge) of one or more electrons. Atoms with a positive charge are known as CATIONS; those with a negative charge are ANIONS.Membrane Lipids: Lipids, predominantly phospholipids, cholesterol and small amounts of glycolipids found in membranes including cellular and intracellular membranes. These lipids may be arranged in bilayers in the membranes with integral proteins between the layers and peripheral proteins attached to the outside. Membrane lipids are required for active transport, several enzymatic activities and membrane formation.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Proline: 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.Drug Stability: The chemical and physical integrity of a pharmaceutical product.Antimicrobial Cationic Peptides: 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.Permeability: Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Amides: Organic compounds containing the -CO-NH2 radical. Amides are derived from acids by replacement of -OH by -NH2 or from ammonia by the replacement of H by an acyl group. (From Grant & Hackh's Chemical Dictionary, 5th ed)Scattering, Radiation: The diversion of RADIATION (thermal, electromagnetic, or nuclear) from its original path as a result of interactions or collisions with atoms, molecules, or larger particles in the atmosphere or other media. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Ion Channel Gating: The opening and closing of ion channels due to a stimulus. The stimulus can be a change in membrane potential (voltage-gated), drugs or chemical transmitters (ligand-gated), or a mechanical deformation. Gating is thought to involve conformational changes of the ion channel which alters selective permeability.Spectroscopy, Fourier Transform Infrared: A spectroscopic technique in which a range of wavelengths is presented simultaneously with an interferometer and the spectrum is mathematically derived from the pattern thus obtained.Hydrogen: The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.Microsomes, Liver: Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.Phosphatidylserines: Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a serine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and serine and 2 moles of fatty acids.Deuterium: Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus.Cell Membrane Permeability: A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.Pressure: A type of stress exerted uniformly in all directions. Its measure is the force exerted per unit area. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Temperature: 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.Nuclear Magnetic Resonance, Biomolecular: NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.Crystallization: The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Structure-Activity Relationship: 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.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Hydrogen-Ion Concentration: 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)Time Factors: Elements of limited time intervals, contributing to particular results or situations.Calcium: A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.Patch-Clamp Techniques: An electrophysiologic technique for studying cells, cell membranes, and occasionally isolated organelles. All patch-clamp methods rely on a very high-resistance seal between a micropipette and a membrane; the seal is usually attained by gentle suction. The four most common variants include on-cell patch, inside-out patch, outside-out patch, and whole-cell clamp. Patch-clamp methods are commonly used to voltage clamp, that is control the voltage across the membrane and measure current flow, but current-clamp methods, in which the current is controlled and the voltage is measured, are also used.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.
The role of proline and glycine in determining the backbone flexibility of a channel-forming peptide. (1/201)
Alamethicin is a helical 20-amino acid voltage-gated channel-forming peptide, which is known to exhibit segmental flexibility in solution along its backbone near alpha-methylalanine (MeA)-10 and Gly-11. In an alpha-helical configuration, MeA at position 10 would normally hydrogen-bond with position 14, but the presence of proline at this position prevents the formation of this interhelical hydrogen bond. To determine whether the presence of proline at position 14 contributes to the flexibility of this helix, two analogs of alamethicin were synthesized, one with proline 14 replaced by alanine and another with both proline 14 and glycine 11 replaced by alanine. The C-termini of these peptides were derivatized with a proxyl nitroxide, and paramagnetic enhancements produced by the nitroxide on the Calpha protons were used to estimate r-6 weighted distances between the nitroxide and the backbone protons. When compared to native alamethicin, the analog lacking proline 14 exhibited similar C-terminal to Calpha proton distances, indicating that substitution of proline alone does not alter the flexibility of this helix; however, the subsequent removal of glycine 11 resulted in a significant increase in the averaged distances between the C- and N-termini. Thus, the G-X-X-P motif found in alamethicin appears to be largely responsible for mediating high-amplitude bending motions that have been observed in the central helical domain of alamethicin in methanol. To determine whether these substitutions alter the channel behavior of alamethicin, the macroscopic and single-channel currents produced by these analogs were compared. Although the substitution of the G-X-X-P motif produces channels with altered characteristics, this motif is not essential to achieve voltage-dependent gating or alamethicin-like behavior. (+info)An alamethicin channel in a lipid bilayer: molecular dynamics simulations. (2/201)
We present the results of 2-ns molecular dynamics (MD) simulations of a hexameric bundle of Alm helices in a 1-palmitoyl-2-oleoylphosphatidylcholine bilayer. These simulations explore the dynamic properties of a model of a helix bundle channel in a complete phospholipid bilayer in an aqueous environment. We explore the stability and conformational dynamics of the bundle in a phospholipid bilayer. We also investigate the effect on bundle stability of the ionization state of the ring of Glu18 side chains. If all of the Glu18 side chains are ionised, the bundle is unstable; if none of the Glu18 side chains are ionized, the bundle is stable. pKA calculations suggest that either zero or one ionized Glu18 is present at neutral pH, correlating with the stable form of the helix bundle. The structural and dynamic properties of water in this model channel were examined. As in earlier in vacuo simulations (Breed et al., 1996 .Biophys. J. 70:1643-1661), the dipole moments of water molecules within the pore were aligned antiparallel to the helix dipoles. This contributes to the stability of the helix bundle. (+info)Preferential transport of glutathione versus glutathione disulfide in rat liver microsomal vesicles. (3/201)
A bi-directional, saturable transport of glutathione (GSH) was found in rat liver microsomal vesicles. GSH transport could be inhibited by the anion transport blockers flufenamic acid and 4, 4'-diisothiocyanostilbene-2,2'-disulfonic acid. A part of GSH taken up by the vesicles was metabolized to glutathione disulfide (GSSG) in the lumen. Microsomal membrane was virtually nonpermeable toward GSSG; accordingly, GSSG generated in the microsomal lumen could hardly exit. Therefore, GSH transport, contrary to previous assumptions, is preferred in the endoplasmic reticulum, and GSSG entrapped and accumulated in the lumen creates the oxidized state of its redox buffer. (+info)Surface binding of alamethicin stabilizes its helical structure: molecular dynamics simulations. (4/201)
Alamethicin is an amphipathic alpha-helical peptide that forms ion channels. An early event in channel formation is believed to be the binding of alamethicin to the surface of a lipid bilayer. Molecular dynamics simulations are used to compare the structural and dynamic properties of alamethicin in water and alamethicin bound to the surface of a phosphatidylcholine bilayer. The bilayer surface simulation corresponded to a loosely bound alamethicin molecule that interacted with lipid headgroups but did not penetrate the hydrophobic core of the bilayer. Both simulations started with the peptide molecule in an alpha-helical conformation and lasted 2 ns. In water, the helix started to unfold after approximately 300 ps and by the end of the simulation only the N-terminal region of the peptide remained alpha-helical and the molecule had collapsed into a more compact form. At the surface of the bilayer, loss of helicity was restricted to the C-terminal third of the molecule and the rod-shaped structure of the peptide was retained. In the surface simulation about 10% of the peptide/water H-bonds were replaced by peptide/lipid H-bonds. These simulations suggest that some degree of stabilization of an amphipathic alpha-helix occurs at a bilayer surface even without interactions between hydrophobic side chains and the acyl chain core of the bilayer. (+info)C-terminally shortened alamethicin on templates: influence of the linkers on conductances. (5/201)
In order to test the influence of chemical modifications designed to allow covalent coupling of channel-forming peptide motifs into variable sized oligomers, a series of alamethicin derivatives was prepared. The building block encompassing the N-terminal 1-17 residues of alamethicin behaved normally in the conductance assay on planar lipid bilayers, albeit at higher concentration and with a slightly reduced voltage-dependence. A linker Ac-K-OCH(2)C(6)H(4)CH(3)p attached via the epsilon amino group of lysine to the C-terminus of alamethicin(1-17) increased membrane affinity. The latter was further enhanced in a dimer and a tetramer in which alamethicin(1-17) chains were tethered to di- or tetra-lysine linkers, respectively, but macroscopic current-voltage curves displayed much reduced voltage-dependencies and reversed hysteresis. An usual behaviour with high voltage-dependence was restored with the modified dimer of alamethicin(1-17) in which alanine separated the two consecutive lysine residues in the linker. Of special interest was the development of a 'negative resistance' branch in macroscopic current-voltage curves for low concentrations of this dimer with the more flexible linker. Single channel events displayed only one single open state with fast kinetics and whose conductance matches that of the alamethicin heptamer or octamer. (+info)A yeast Golgi E-type ATPase with an unusual membrane topology. (6/201)
E-type ATPases are involved in many biological processes such as modulation of neural cell activity, prevention of intravascular thrombosis, and protein glycosylation. In this study, we show that a gene of Saccharomyces cerevisiae, identified by similarity to that of animal ectoapyrase CD39, codes for a new member of the E-type ATPase family (Apy1p). Overexpression of Apy1p in yeast cells causes an increase in intracellular membrane-bound nucleoside di- and triphosphate hydrolase activity. The activity is highest with ADP as substrate and is stimulated similarly by Ca (2+), Mg(2+), and Mn(2+). The results also indicate that Apy1p is an integral membrane protein located predominantly in the Golgi compartment. Sequence analysis reveals that Apy1p contains one large NH(2)-terminal hydrophilic apyrase domain, one COOH-terminal hydrophilic domain, and two hydrophobic stretches in the central region of the polypeptide. Although no signal sequence is found at the NH(2)-terminal portion of the protein and no NH(2)-terminal cleavage of the protein is observed, demonstrated by the detection of NH(2)-terminal tagged Apy1p, the NH(2)-terminal domain of Apylp is on the luminal side of the Golgi apparatus, and the COOH-terminal hydrophilic domain binds to the cytoplasmic face of the Golgi membrane. The second hydrophobic stretch of Apy1p is the transmembrane domain. These results indicate that Apylp is a type III transmembrane protein; however, the size of the Apy1p extracytoplasmic NH(2) terminus is much larger than those of other type III transmembrane proteins, suggesting that a novel translocation mechanism is utilized. (+info)The ion-channel activity of longibrachins LGA I and LGB II: effects of pro-2/Ala and gln-18/Glu substitutions on the alamethicin voltage-gated membrane channels. (7/201)
Longibrachins LGA I (Ac Aib Ala Aib Ala Aib(5) Ala Gln Aib Val Aib(10) Gly Leu Aib Pro Val(15) Aib Aib Gln Gln Pheol(20), with Aib: alpha-aminoisobutyric acid, pheol: phenylalaninol) and LGB II are two homologous 20-residue long-sequence peptaibols isolated from the fungus Trichoderma longibrachiatum that differ between them by a Gln-18/Glu substitution. They distinguish from alamethicin by a Pro-2 for Ala replacement, which allowed to examine for the first time with natural Aib-containing analogues, the effect of Pro-2 on the ion-channel properties exhibited by alamethicin. The influence of these structural modifications on the voltage-gated ion-channel forming activity of the peptides in planar lipid bilayers were analysed. The general 'barrel-stave' model of ion-channel activity, already described for alamethicin, was preserved with both longibrachins. The negatively charged LGB II promoted higher oligomerisation levels, which could presumably dilute the repulsive effect of the negative Glu ring near the entrance of the channel and resulted in lower lifetimes of the substates, confirming the strong anchor of the peptide C-terminus at the cis-interface. Reduction of the channel lifetimes was observed for the longibrachins, compared to alamethicin. This argues for a better stabilisation of the channels formed by peptaibols having a proline at position 2, which results in better anchoring of the peptide monomer N-terminus at the trans-bilayer interface. Qualitative assays of the temperature dependence on the neutral longibrachin channel properties demonstrated a high increase of channel lifetimes and a markedly reduced voltage-sensitivity when the temperature was decreased, showing that such conditions may allow to study the channel-forming properties of peptides leading to fast current fluctuations. (+info)Voltage-dependent interaction of the peptaibol antibiotic zervamicin II with phospholipid vesicles. (8/201)
The effect of a transmembrane potential on ion channel formation by zervamicin II (ZER-II) was studied in a vesicular model system. The dissipation of diffusion potential caused by addition of ZER-II to small phosphatidylcholine vesicles was monitored using fluorescent (Safranine T) and optical (Oxonol YI) probes. Cis-positive potentials facilitated channel formation, while at cis-negative potentials, ion fluxes were inhibited. A potential-independent behavior of ZER-II was observed at high peptide concentrations, most likely due to its membrane modifying property. (+info)The most widely known peptaibol is alamethicin. J. K. Chugh & B. A. Wallace (20 February 2001). "Peptaibols: models for ion ...
Gramicidin and alamethicin had been popular starting points for selective modifications. The above diagram illustrates one ... The latter, demonstrated in natural channels such as alamethicin, is rarely encountered in synthetic ion channels. They may be ... "Alamethicin−Leucine Zipper Hybrid Peptide: A Prototype for the Design of Artificial Receptors and Ion Channels". Journal of the ...
Marsh, Derek; Jost, Micha; Peggion, Cristina; Toniolo, Claudio (2007). "TOAC spin labels in the backbone of alamethicin: EPR ...
Both of these amino acids are found in peptidic lantibiotics such as alamethicin. However, in plants, 1-aminocyclopropane-1- ...
It is contained in some antibiotics of fungal origin, e.g. alamethicin and some lantibiotics. It is not one of the ...
Penicillin, cephalosporins, fusafungine, usnic acid, fusidic acid, fumagillin, brefeldin A, verrucarin A, alamethicin, are ...
Fox, R.O.; Richards, F.M. (1982). "A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5- ... the ion-channel-forming alamethicin (PDB: 1AMT) (Fox & Richards 1982), and mutants of ribonuclease S (e.g., PDB: 1RBD;PDB: ...
Toisc go bhfuil an liosta bunaithe ar an leagan Béarla i 'Wikipedia en' beidh an leagan Béarla ar dtús agus an leagan Gaeilge ina dhiaidh. Tá súil agam, nuair atá méid áirithe den liosta aistrithe go Gaeilge gur féidir liosta i nGaeilge a chumadh nó i nGaeilge agus i mBéarla. ...
Subsequent discoveries included alamethicin, aphidicolin, brefeldin A, Cephalosporin, cerulenin, citromycin, eupenifeldin, ...
Anisomycin, Thiolutin, Wortmannin, K252a, Staurosporine, K252C, Bafilomycin, Alamethicin, Leptomycin, A23187, Chelerythrine, ...
Family 1.D.3 The Channel-Forming Syringopeptin Family 1.D.4 The Tolaasin Channel-forming Family 1.D.5 The Alamethicin or ...
Aequorin Aflatoxin Agar Alamethicin Alanine Albumins Aldosterone Aleurone Alpha-amanitin Allantoin Allethrin α-Amanatin, see ...
... alamethicin MeSH D04.345.566.050 --- amanitins MeSH D04.345.566.075 --- bacitracin MeSH D04.345.566.142 --- capreomycin sulfate ...
... alamethicin MeSH D12.644.641.050 --- amanitins MeSH D12.644.641.075 --- bacitracin MeSH D12.644.641.142 --- capreomycin sulfate ...
Explore structures of Alamethicin at the protein data bank Alamethicin in Norine From "A voltage-gated ion channel model ... Alamethicin biosynthesis is hypothesized to be catalyzed by alamethicin synthase, a Nonribosomal peptide synthase (NRPS) first ... Alamethicin product page from Fermentek Rindfleisch, H.; Kleinkauf, H. (1976-03-01). "Biosynthesis of alamethicin". FEBS ... Alamethicin is a channel-forming peptide antibiotic, produced by the fungus Trichoderma viride. It belongs to peptaibol ...
"TOAC spin labels in the backbone of alamethicin: EPR studies in lipid membranes". Biophys. J. 92 (2): 473-481. doi:10.1529/ ...
"TOAC spin labels in the backbone of alamethicin: EPR studies in lipid membranes". Biophys. J. 92 (2): 473-481. PMC 1751395 ...
Alamethicin remains the prototype of this class and its biophysical properties (mostly focussing on channel- or pore-formation ... Alamethicin remains the prototype of this class and its biophysical properties (mostly focussing on channel- or pore-formation ... Keywords:Antimicrobial peptides, peptaibols, alamethicin, planar lipid bilayers. Abstract: In this review, the antimicrobial ...
Explore structures of Alamethicin at the protein data bank Alamethicin in Norine From "A voltage-gated ion channel model ... Alamethicin biosynthesis is hypothesized to be catalyzed by alamethicin synthase, a Nonribosomal peptide synthase (NRPS) first ... Alamethicin product page from Fermentek Rindfleisch, H.; Kleinkauf, H. (1976-03-01). "Biosynthesis of alamethicin". FEBS ... Alamethicin is a channel-forming peptide antibiotic, produced by the fungus Trichoderma viride. It belongs to peptaibol ...
Potential-dependent conductances in lipid membranes containing alamethicin Message Subject (Your Name) has sent you a message ... From the properties of lipid membranes containing alamethicin in a wide variety of electrolytes, and from other evidence, it is ... Potential-dependent conductances in lipid membranes containing alamethicin. L. G. M. Gordon, D. A. Haydon ... that alamethicin forms transient pores of some 0.6 nm in diameter and that, for small inorganic ions, these are poorly ...
... rupture and fuse in response to the addition of both melittin and alamethicin. In the case of alamethicin, but not melittin, ... Effect of α-helical peptides on liposome structure: A comparative study of melittin and alamethicin. Wessman, Per Uppsala ... By means of a competitive binding assay we furthermore show that alamethicin, in line with earlier findings for melittin, ... Melittin, Alamethicin, Magainin, Liposomes, Affinity, Cryo-transmission electron microscopy National Category Physical ...
"Voltage-Dependent Pore Formation and Antimicrobial Activity by Alamethicin and Analogues, The Journal of Membrane Biology" on ... Voltage-Dependent Pore Formation and Antimicrobial Activity by Alamethicin and Analogues. Duclohier, H.; Wróblewski, H. ... Voltage-Dependent Pore Formation and Antimicrobial Activity by Alamethicin and Analogues Duclohier, H. ; Wróblewski, H. 2001-11 ... The demonstration of ar- alamethicin [33] was a landmark, from which new struc- tificial membrane excitability developed by ...
In a 20-ns simulation of a hexameric alamethicin bundle, the main motions are those of individual helices, not of the bundle as ... We have used extended molecular dynamics simulations of alamethicin bundles consisting of 4, 5, 6, 7, and 8 helices in a ... shows that water orientation inside the alamethicin channels is sensitive to the algorithms used. In all cases, water ordering ... Alamethicin is an antimicrobial peptide that forms stable channels with well-defined conductance levels. ...
... Mark Abraham Mark.Abraham at anu.edu.au Tue Nov 6 11:12:45 CET 2007 *Previous message: [gmx-users ...
Alamethicin forms voltage-gated ion channels that have moderate cation-selectivity. The enhancement of the cation-selectivity ... by introducing negatively charged residues at positions 7 and 18 has been studied using the tethered homodimers of alamethicin ... Alamethicin forms voltage-gated ion channels that have moderate cation-selectivity. The enhancement of the cation-selectivity ... Ion channels of N-terminally linked alamethicin dimers: enhancement of cation-selectivity by substitution of Glu for Gln at ...
Alamethicin LKT Labs. Alamethicin is a peptabiol peptide initially produced by species of Trichoderma. Alamethicin is an ...
Alamethicin. A rich model for channel behavior journal, January 1984 * Hall, J. E.; Vodyanoy, I.; Balasubramanian, T. M. ... "Reversed" alamethicin conductance in lipid bilayers journal, April 1991 * Taylor, R. J.; de Levie, R. ...
Alamethicin. *Alamethicin is a peptide.. *Alamethicin is a well-studied channel-forming peptide that has a prototypical ... ALAMETHICIN. ALBENDAZOLE. ALFUZOSIN. ALKYLATING AGENT. ALLOPURINOL. ALPHA HYDROXY ACID. ALPHA BLOCKER. AMIDRINE. AMILORIDE. ... In this model alamethicin helices associate to form a bundle with a central lumen, like a barrel made of helical peptides as ...
Biophysical changes induced by cholesterol on phosphatidylcholine artificial biomembranes containing alamethicin oligomers. ...
Infrared Spectroscopy as a Probe for the Development of Secondary Structure in the Amino-Terminal Segment of Alamethicin ... Interest in the stereochemistry of Aib containing peptides, stems from the fact that alamethicin [7,8] and the related ... Here, we report the results of an infrared spectroscopic study of synthetic alamethicin fragments and demonstrate the ... Infrared Spectroscopy as a Probe for the Development of Secondary Structure in the Amino-Terminal Segment of Alamethicin. In: ...
A comparison of alamethicin, gramicidin A, melittin and tetraacetyl melittin. (deposited 20 May 2010 06:48) * Effects of ... A comparison of alamethicin, gramicidin A, melittin and tetraacetyl melittin. (deposited 20 May 2010 05:02) [Currently ... A comparison of alamethicin, gramicidin A, melittin and tetraacetyl melittin. In: Biochemistry International, 11 (3). 357 -363 ... At low Pi (2.5 mM) the order of uncoupling efficiencies is gramicidin A much greater than alamethicin greater than tetraacetyl ...
Alamethicin. A-1286. Options. 5 mg $160.15. 10 mg $288.72. 50 mg $664.59. ...
Alamethicin suppresses methanogenesis and promotes acetogenesis in bioelectrochemical systems.. Zhu X, Siegert M, Yates MD, ...
Interaction of a helical peptide with membrane: Study of alamethicin Wu, Yili (1994) Alamethicin is a transmembrane ion channel ... reports the studies of the structure and mechanism of peptide-induced membrane pores by antimicrobial peptide alamethicin and ...
... the omission of alamethicin. Alamethicin was used previously (23) to open pores in the membrane to allow NADH to access all of ... Alamethicin has been reported to sequester membrane-bound fatty acids (30) so it may sequester quinones also, and to induce ... 2017) Alamethicin can capture lipid-like molecules in the membrane. J Chem Phys 146:011103. ... 2014) Antimicrobial peptide alamethicin insertion into lipid bilayer: A QCM-D exploration. Colloids Surf B Biointerfaces 116: ...
Voltage-dependent pore activity of the peptide alamethicin correlated with incorporation in the membrane: salt and cholesterol ... Thermodynamic analysis of incorporation and aggregation in a membrane: application to the pore-forming peptide alamethicin. ... Incorporation kinetics in a membrane, studied with the pore-forming peptide alamethicin. ...
जे.सी.-1 की विशिष्टता और सूजन संकेतों 1 सुक्ष्ममापी CCCP और 5 ग्राम / एमएल alamethicin (माइक्रोबियल विष) के साथ परीक्षण किया ...
MtPTP aktivasyonu takiben, 1 mM EGTA, 1 uM CCCP ve 5 ug / ml alamethicin ile sırasıyla Fura FF, JC-1 ve şişme sinyallerin ... JC-1 Özgünlük ve şişme sinyaller 1 uM CCCP ve 5 mg / ml alamethicin (mikrobiyal toksin) ile test edildi. ...
alamethicin. American Laryngological Association. American Lung Association. delta-aminolevulinic acid, see there. Association ...
Alamethicin channel conductance modified by lipid charge. Vicente Manuel Aguilella Fernández, Sergey M. Bezrukov. EUROPEAN ... Lipid Charge Effects in Alamethicin-induced conductance. Vicente Manuel Aguilella Fernández, S.M. Bezrukov. Biophysical Society ...
Alamethicin. A-1286-5mg. $353.00 AG Scientific. CAS NUMBER = 27061-78-5 ...
Metabolic Assessment in Alamethicin-Activated Liver Microsomes: Co-activating CYPs and UGTs ...
- Alamethicin remains the prototype of this class and its biophysical properties (mostly focussing on channel- or pore-formation in planar lipid bilayers) were and are still intensively studied. (eurekaselect.com)
- Initially, we show that the antimicrobial peptides melittin, alamethicin and magainin 2, in spite of their very different physico-chemical properties and suggested modes of action on membranes, all have high affinity to lipodisks. (diva-portal.org)
- Observations made with these peptides are distinct as seen from data obtained with the hydrophobic peptide alamethicin. (mdpi.com)
- Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin. (tcdb.org)
- This article is concerned primarily with the mechanism of the potential-dependent conductance induced in artificial lipid membranes by the cyclic polypeptide antibiotic alamethicin. (royalsocietypublishing.org)
- The natural alpha-helical peptide antibiotic alamethicin forms voltage-gated ion channels in lipid membranes. (lifl.fr)
- Interaction of the peptide antibiotic alamethicin with bilayer- and non-bilayer-forming lipids: Influence of increasing alamethicin concentration on the lipids supramolecular structures. (mpg.de)
- Alamethicin is an antimicrobial peptide that forms stable channels with well-defined conductance levels. (ox.ac.uk)
- We have used extended molecular dynamics simulations of alamethicin bundles consisting of 4, 5, 6, 7, and 8 helices in a palmitoyl-oleolyl-phosphatidylcholine bilayer to evaluate and analyze channel models and to link the models to the experimentally measured conductance levels. (ox.ac.uk)
- For two AMPs, alamethicin and novicidin, we observe that the majority of the lipids remain in a planar bilayer conformation but that a number of lipids are involved in the peptide anchoring.These lipids display reduced dynamics.Our study supports previous studies showing that alamethicin adopts a transmembrane arrangement without significant disturbance of the surrounding lipids, while novicidin forms toroidal pores at high concentrations leading to more extensive membrane disturbance. (nih.gov)
- For two AMPs, alamethicin and novicidin, we observe that the majority of the lipids remain in a planar bilayer conformation but that a number of lipids are involved in the peptide anchoring. (nih.gov)
- Neutron in‐plane scattering intensity of alamethicin pores in DLPC bilayer at P / L =1/10 hydrated with D 2 O (data +) or with H 2 O (data o). (els.net)
- Bilayer recordings: Alamethicin single channel conductances. (nanion.de)
- Alamethicin is a channel-forming peptide antibiotic, produced by the fungus Trichoderma viride. (wikipedia.org)
- Alamethicin is a peptabiol peptide initially produced by species of Trichoderma. (thomassci.com)
- From the properties of lipid membranes containing alamethicin in a wide variety of electrolytes, and from other evidence, it is concluded that the polypeptide reacts to the electric field more probably because it has a large dipole moment than because it binds ions. (royalsocietypublishing.org)
- Alamethicin remains the prototype of this class and its biophysical properties (mostly focussing on channel- or pore-formation in planar lipid bilayers) were and are still intensively studied. (eurekaselect.com)
- Klinke, N., Goldermann, M. and Hanke, W.: The properties of alamethicin incorporated into planar lipid bilayers under the influence of microgravity. (uni-bremen.de)
- cholesterol change their shape, rupture and fuse in response to the addition of both melittin and alamethicin. (diva-portal.org)
- In the context of the molecular shape concept, the properties of lipopeptides, including surfactins, are shortly presented, and comparisons with the hydrophobic alamethicin sequence are made. (springer.com)
- The absence of response in yeast mitochondria was not simply due to structural limitations, since large-amplitude swelling occurred in the presence of alamethicin, a hydrophobic, helical peptide, forming voltage-sensitive ion channels in lipid membranes. (sigmaaldrich.com)
- Alamethicin adopts transmembrane conformations (Fig. 6d) and novicidin uses the lipids to form toroidal pores with the lipid (Fig. 6e). (nih.gov)
- Alamethicin is a channel-forming antibiotic known to increase the permeability of biological membranes through the creation of transmembrane pores up to 20 A in diameter, providing ready access for NADH to enter intact mitochondria, as previously demonstrated with rat skeletal muscle homogenate ( 10 ) and rat heart mitochondria ( 11 ). (diabetesjournals.org)
- The possibility that taurocholate effects may result from non-specific activation of the overt enzyme was excluded by employing the channel-forming peptide alamethicin to effect permeabilization, and by varying the mode of delivery of diacylglycerol substrate to the microsomal membranes. (biochemj.org)
- Permeabilization using alamethicin gave a slightly higher latent/overt ratio for DGAT. (biochemj.org)
- A comparison of alamethicin, gramicidin A, melittin and tetraacetyl melittin. (iisc.ac.in)
- At low Pi (2.5 mM) the order of uncoupling efficiencies is gramicidin A much greater than alamethicin greater than tetraacetyl melittin greater than melittin. (iisc.ac.in)
- Voltage-Dependent Pore Formation and Antimicrobial Activity by Alamethicin and Analogues Duclohier, H. (deepdyve.com)
- Data of six different peptide/lipid systems are shown: alamethicin in diphytanoyl phosphatidylcholine ( DPhPC ), alamethicin in a mixture of dioleoyl phosphatidylcholine ( DOPC ) and dioleoyl phosphatidylethanolamine ( DOPE ), melittin in DPhPC , melittin in DOPC , melittin in palmitoyl‐oleoyl phosphatidylcholine ( POPC ), and melittin in dieicosenoyl phosphatidylcholine (DiC20:1PC). (els.net)
- Explore structures of Alamethicin at the protein data bank Alamethicin in Norine From "A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution. (wikipedia.org)
- Note the orientation of the protein so that its 'superstructure' is housed ouside the tethaPlasm]] Many proteins comprise lipohilic and hydrophilic sections and these affect the [http://en.wikipedia.org/wiki/Protein_tertiary_structure tertiary protein structure]. (edaq.com)
- Although there are several sequences of the alamethicin peptide accepted, evidence suggests these all follow the general NRPS mechanism with small variations at select amino acids. (wikipedia.org)
- Here, we report the results of an infrared spectroscopic study of synthetic alamethicin fragments and demonstrate the development of a $3_{10}$ helical structure at the amino-terminus of the antibiotic. (iisc.ac.in)
- Single-channel electrical recordings of the peptide alamethicin and of the proteoliposome-delivered potassium channel KcsA demonstrate channel conductance with low noise, made possible by the small capacitance of the 50 µm thick SU8 septum, which is only thinned around the aperture, and unimpeded proteoliposome fusion, enabled by the large aperture diameter. (soton.ac.uk)
- Analysis and evaluation of channel models: simulations of alamethicin. (ox.ac.uk)
- The activity of rotenone-sensitive NADH:O 2 oxidoreductase, reflecting the overall activity of the respiratory chain, was measured in a mitochondrial fraction by a novel method based on providing access for NADH to intact mitochondria via alamethicin, a channel-forming antibiotic. (diabetesjournals.org)