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Alpha-helical cationic antimicrobial peptides: relationships of structure and function

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

http://www.wikidata.org/entity/Q37825833

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The effect of amidation on the behaviour of antimicrobial peptides The Potential Use of Natural and Structural Analogues of Antimicrobial Peptides in the Fight against Neglected Tropical Diseases Insights into the antimicrobial properties of hepcidins: advantages and drawbacks as potential therapeutic agents Antimicrobial peptides for therapeutic applications: a review Peptidomimetics as a new generation of antimicrobial agents: current progress Structural basis for antimicrobial activity of lasiocepsin Big defensins, a diverse family of antimicrobial peptides that follows different patterns of expression in hemocytes of the oyster Crassostrea gigas Hp1404, a new antimicrobial peptide from the scorpion Heterometrus petersii Host-defense peptides with therapeutic potential from skin secretions of frogs from the family pipidae The PDB database is a rich source of alpha-helical anti-microbial peptides to combat disease causing pathogens.Recent advances in developing insect natural products as potential modern day medicines Role of helicity of α-helical antimicrobial peptides to improve specificity.The study of single anticancer peptides interacting with HeLa cell membranes by single molecule force spectroscopy.Deciphering the magainin resistance process of Escherichia coli strains in light of the cytosolic proteome Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera.Peptide therapeutics for treating ocular surface infections Targeting Mycobacterium tuberculosis and other microbial pathogens using improved synthetic antibacterial peptides.Investigating specific bacterial resistance to AMPs by using a magainin I-resistant Escherichia coli model.Characterization of antibacterial and hemolytic activity of synthetic pandinin 2 variants and their inhibition against Mycobacterium tuberculosis.Exploring the pharmacological potential of promiscuous host-defense peptides: from natural screenings to biotechnological applications.Applications of circular dichroism for structural analysis of gelatin and antimicrobial peptides.Effect of repetitive lysine-tryptophan motifs on the eukaryotic membrane.Mechanism of action and initial evaluation of a membrane active all-D-enantiomer antimicrobial peptidomimetic Contribution of Amphipathicity and Hydrophobicity to the Antimicrobial Activity and Cytotoxicity of β-Hairpin Peptides New and alternative approaches to tackling antibiotic resistance.Activity of Scorpion Venom-Derived Antifungal Peptides against Planktonic Cells of Candida spp. and Cryptococcus neoformans and Candida albicans Biofilms Transcriptome analysis in venom gland of the predatory giant ant Dinoponera quadriceps: insights into the polypeptide toxin arsenal of hymenopterans.Non-disulfide-Bridge Peptide 5.5 from the Scorpion Hadrurus gertschi Inhibits the Growth of Mycobacterium abscessus subsp. massiliense.Antimicrobial peptides: their physicochemical properties and therapeutic application.Antimicrobial peptides: therapeutic potentials.Defense peptides: recent developments.Structure-Activity Relationships of Insect Defensins.Δ-Myrtoxin-Mp1a is a Helical Heterodimer from the Venom of the Jack Jumper Ant that has Antimicrobial, Membrane-Disrupting, and Nociceptive Activities.Enhanced Antimicrobial Activity of AamAP1-Lysine, a Novel Synthetic Peptide Analog Derived from the Scorpion Venom Peptide AamAP1.Transformation of the naturally occurring frog skin peptide, alyteserin-2a into a potent, non-toxic anti-cancer agent.Bacteria-Assisted Activation of Antimicrobial Polypeptides by a Random-Coil to Helix Transition.A peptide from human β thymosin as a platform for the development of new anti-biofilm agents for Staphylococcus spp. and Pseudomonas aeruginosa.K1K8: an Hp1404-derived antibacterial peptide.Antimicrobial activity of four cationic peptides immobilised to poly-hydroxyethylmethacrylate.Antimicrobial Peptides from the Aurein Family Form Ion-Selective Pores in Bacillus subtilis.

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P2860

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

http://www.wikidata.org/entity/Q37825833

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 06 February 2010

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

@en

Alpha-helical cationic antimicrobial peptides: relationships of structure and function.

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type

label

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

@en

Alpha-helical cationic antimicrobial peptides: relationships of structure and function.

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prefLabel

Alpha-helical cationic antimicrobial peptides: relationships of structure and function

@en

Alpha-helical cationic antimicrobial peptides: relationships of structure and function.

@nl

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Alpha-helical cationic antimicrobial peptides: relationships of structure and function

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Jinfeng Huang

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Yibing Huang

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Yuxin Chen

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P2860

MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain.

Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor

Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Determination of stereochemistry stability coefficients of amino acid side-chains in an amphipathic alpha-helix.

Antimicrobial peptides protect coho salmon from Vibrio anguillarum infections.

All-D amino acid-containing channel-forming antibiotic peptides.

Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes.

Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides.

Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells.

Amphipathic, alpha-helical antimicrobial peptides.

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s13238-010-0004-3

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143-152

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scholarly article

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10.1007/S13238-010-0004-3

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