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
Ion Channels
Melitten
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
Phosphatidylcholines
Octanes
Tetrathionic Acid
Membranes, Artificial
Trichoderma
Spin Labels
Electrochemistry
Protein Structure, Secondary
Models, Molecular
Phosphatidylethanolamines
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
Membrane Fluidity
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
Amino Acid Sequence
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
Water
Mathematics
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
Hydrogen Bonding
Magnetic Resonance Spectroscopy
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
Models, Structural
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
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
Computer Simulation
Physicochemical Phenomena
Models, Chemical
Chemistry, Physical
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
Methanol
Potentiometry
Molecular Probes
Ions
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
Proline
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
Cell Membrane
Amides
Scattering, Radiation
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
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
Phosphatidylserines
Deuterium
Cell Membrane Permeability
Pressure
Temperature
Nuclear Magnetic Resonance, Biomolecular
Crystallization
Structure-Activity Relationship
Membrane Proteins
Hydrogen-Ion Concentration
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.
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)
Structural and biophysical properties of a synthetic channel-forming peptide: designing a clinically relevant anion selective...
Ion channels of N-terminally linked alamethicin dimers: enhancement of cation-selectivity by substitution of Glu for Gln at...
The design, synthesis and characterisation of channel-forming peptides
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Alamethicin
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 ...
Peptaibol
The most widely known peptaibol is alamethicin. Chugh JK, Wallace BA (August 2001). "Peptaibols: models for ion channels". ...
Halovir
"The antibacterial activity of alamethicins and zervamicins". Journal of Applied Bacteriology. 63 (4): 293-298. doi:10.1111/j. ...
Synthetic ion channels
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 ...
Orientations of Proteins in Membranes database
Marsh, Derek; Jost, Micha; Peggion, Cristina; Toniolo, Claudio (2007). "TOAC spin labels in the backbone of alamethicin: EPR ...
Amino acid
Both of these amino acids are found in peptidic lantibiotics such as alamethicin. However, in plants, 1-aminocyclopropane-1- ...
Fungal isolate
Penicillin, cephalosporins, fusafungine, usnic acid, fusidic acid, fumagillin, brefeldin A, verrucarin A, alamethicin, are ...
Frederic M. Richards
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: ...
2-Aminoisobutyric acid
It is rare in nature, having been only found in meteorites, and some antibiotics of fungal origin, such as alamethicin and some ...
Medicinal fungi
Subsequent discoveries included alamethicin, aphidicolin, brefeldin A, cephalosporin, cerulenin, citromycin, eupenifeldin, ...
Fermentek
Anisomycin, Thiolutin, Wortmannin, K252a, Staurosporine, K252C, Bafilomycin, Alamethicin, Leptomycin, A23187, Chelerythrine, ...
Transporter Classification Database
Family 1.D.3 The Channel-Forming Syringopeptin Family 1.D.4 The Tolaasin Channel-forming Family 1.D.5 The Alamethicin or ...
List of biomolecules
Aequorin Aflatoxin Agar Alamethicin Alanine Albumins Aldosterone Aleurone Alpha-amanitin Alpha-MSH (Melaninocyte stimulating ...
List of MeSH codes (D04)
... alamethicin MeSH D04.345.566.050 - amanitins MeSH D04.345.566.075 - bacitracin MeSH D04.345.566.142 - capreomycin sulfate MeSH ...
List of MeSH codes (D12.644)
... alamethicin MeSH D12.644.641.050 - amanitins MeSH D12.644.641.075 - bacitracin MeSH D12.644.641.142 - capreomycin sulfate MeSH ...
IMSEAR at SEARO: Interactions of the channel forming peptide alamethicin with artificial and natural membranes.
Alamethicin is shown to function as an uncoupler of oxidative phosphorylation in rat liver mitochondria. The influence of ... Alamethicin and related α-aminoisobutyric acid peptides form transmembrane channels across lipid bilayers. This article briefly ... Alamethicin. membrane channels. mitochondrial uncouplers. mitochondrial inhibitors. peptide-lipid interactions. membranes. ... Das Manoj K, Balaram P. Interactions of the channel forming peptide alamethicin with artificial and natural membranes. Journal ...
MESH TREE NUMBER CHANGES - 2008 MeSH
Nanion Technologies - Products - Port-a-Patch
Alamethicin - Bilayer Recordings Port-a-Patch and Vesicle Prep Pro data and applications:. Data were kindly provided by M. ... reveals multiple non-equidistant conductance levels due to formation of alamethicin oligomers in the bilayer. Alamethicin ... Bilayer recordings: Alamethicin single channel conductances. Recordings from a GUV prepared bilayer in 85 mM KCl at -140 mV. ... 2006 - High-resolution electrophysiology on a chip: Transient dynamics of alamethicin channel formation Port-a-Patch and ...
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The final incubation mixture (100 μl) included 5 mM MgCl2, 10 μg of alamethicin/mg of protein, 50 mM Tris buffer, pH 8.4, 2 mM ... The final incubation mixture (100 μl) included 5 mM MgCl2, 10 μg of alamethicin/mg of protein, 50 mM Tris buffer, pH 7.4 or 8.4 ... The final incubation mixture (100 μl) included 5 mM MgCl2, 10 μg of alamethicin/mg of protein, 50 mM Tris buffer, pH 7.4 or 8.4 ... 10 μg alamethicin/mg of protein, 50 mM Tris buffer, pH 7.4, 2 mM UDPGA (including 0.3 μCi of the labeled cofactor), and 0.5 mg ...
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Cyclodextrin scaffolded alamethicin with highly efficient channel-forming properties. Journal of Peptide Science, 16, 148. ... Cyclodextrin Scaffolded Alamethicin with Highly Efficient Channel-forming Properties. Poster session presented at 31st European ... A Combined Liquid-State NMR and Molecular Dynamics Study of Alamethicin in DMPC/DHPC Bicelles. Journal of Physical Chemistry ... Cyclodextrin-Scaffolded Alamethicin with Remarkably Efficient Membrane Permeabilizing Properties and Membrane Current ...
DeCS
MESH TREE NUMBER CHANGES - 2008 MeSH
MESH TREE NUMBER CHANGES - 2008 MeSH
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MESH TREE NUMBER CHANGES - 2008 MeSH
MESH TREE NUMBER CHANGES - 2008 MeSH
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Lipid bilayers3
- Alamethicin and related α-aminoisobutyric acid peptides form transmembrane channels across lipid bilayers. (who.int)
- This article briefly reviews studies on the effect of alamethicin on lipid phase transitions in lipid bilayers and on mitochondrial oxidative phosphorylation. (who.int)
- Fluorescence polarization studies, employing 1,6-diphenyl-1,3,5-hexatriene as a probe, suggest that alamethicin fluidizes lipid bilayers below the phase transition t-emperature, but has little effect above the gel-liquid crystal transition point. (who.int)
Membrane1
- Time-dependent changes in respiration rates following peptide addition are rationalized in terms of alamethicin interactions with mitochondrial membrane components. (who.int)
Peptide1
- IMSEAR at SEARO: Interactions of the channel forming peptide alamethicin with artificial and natural membranes. (who.int)
Peptides2
- Simulations of Membrane-Disrupting Peptides I: Alamethicin Pore Stability and Spontaneous Insertion. (nih.gov)
- Alamethicin peptides are shown as orange (hydrophobic residues) and green (polar and charged residues) ribbons, water molecules are distinguished as in the pore (cyan spheres) or non-pore (light gray spheres), and the lipid phosphorus are dark gray spheres. (nih.gov)
Antibiotic1
- The antibiotic peptaibol alamethicin from Trichoderma permeabilises Arabidopsis root apical meristem and epidermis but is antagonised by cellulase-induced resistance to alamethicin. (mpg.de)
Membranes1
- We therefore examined commercial polymyxin B, ticles accumulate at both the outer and inner membranes of gramicidin A and alamethicin (from Sigma-Aldrich, Buchs, bacteria (13). (medicpdf.com)
Conductance1
- However, when the salt concentration in the membrane-bathing solution is decreased, the surface charge manifests itself as an increase in the conductance of the first two channel levels that correspond to the smallest conductive alamethicin aggregates. (nih.gov)
Fluctuations2
- Studying the influence of ambient noise on signal transfer through the ion channels of alamethicin, we found that external voltage fluctuations could play a constructive role via stochastic resonance. (nih.gov)
- With this system we resolve single-channel currents from several types of bacterial ion channels, including fluctuations of a single alamethicin channel at a bandwidth of 1 MHz which represent the fastest single-ion-channel recordings reported to date. (columbia.edu)
Channel1
- Bilayer recordings: Alamethicin single channel conductances. (nanion.de)
Chemical2
Found1
- Both these amino acids are both found in peptidic lantibiotics such as alamethicin . (wikidoc.org)