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Open AccessJournal ArticleDOI

Describing the mechanism of antimicrobial peptide action with the interfacial activity model.

William C. Wimley
- 15 Oct 2010 - 
- Vol. 5, Iss: 10, pp 905-917
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TLDR
An "interfacial activity model" is proposed, which is based on an experimentally testable molecular image of AMP-membrane interactions, which may be useful in driving engineering and design of novel AMPs.
Abstract
Antimicrobial peptides (AMPs) have been studied for three decades, and yet a molecular understanding of their mechanism of action is still lacking. Here we summarize current knowledge for both synthetic vesicle experiments and microbe experiments, with a focus on comparisons between the two. Microbial experiments are done at peptide to lipid ratios that are at least 4 orders of magnitude higher than vesicle-based experiments. To close the gap between the two concentration regimes, we propose an “interfacial activity model”, which is based on an experimentally testable molecular image of AMP–membrane interactions. The interfacial activity model may be useful in driving engineering and design of novel AMPs.

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Designing antimicrobial peptides: form follows function

TL;DR: In this article, advanced computer assisted design strategies that address the difficult problem of relating primary sequence to peptide structure, and are delivering more potent, cost-effective, broad-spectrum peptides as potential next-generation antibiotics.
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The expanding scope of antimicrobial peptide structures and their modes of action.

TL;DR: Several intact proteins or protein fragments are now being shown to have inherent antimicrobial activity, suggesting a better understanding of the structure-activity relationships of AMPs is required to facilitate the rational design of novel antimicrobial agents.
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Antimicrobial Peptides: Diversity, Mechanism of Action and Strategies to Improve the Activity and Biocompatibility In Vivo

TL;DR: The diversity, history and the various mechanisms of action of AMPs are discussed, and some of the recent strategies developed to improve the activity and biocompatibility of AMP are reviewed.
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Antimicrobial Peptides: Successes, Challenges and Unanswered Questions

TL;DR: The state of the field is discussed and some questions that, if answered, could speed the discovery of clinically useful peptide antibiotics are posed.
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Intracellular Delivery by Membrane Disruption: Mechanisms, Strategies, and Concepts.

TL;DR: Techniques for membrane disruption-based intracellular delivery from 1911 until the present achieve rapid, direct, and universal delivery of almost any cargo molecule or material that can be dispersed in solution.
References
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Journal ArticleDOI

Agar and broth dilution methods to determine the minimal inhibitory concentration (MIC) of antimicrobial substances

TL;DR: The aim of broth and agar dilution methods is to determine the lowest concentration of the assayed antimicrobial agent (minimal inhibitory concentration, MIC) that, under defined test conditions, inhibits the visible growth of the bacterium being investigated.
Journal ArticleDOI

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

TL;DR: A family of peptides with broad-spectrum antimicrobial activity has been isolated from the skin of the African clawed frog Xenopus laevis and appears to represent a previously unrecognized class of vertebrate antimicrobial activities.
Journal ArticleDOI

Vesicles of variable sizes produced by a rapid extrusion procedure

TL;DR: Freeze-fracture electron microscopy revealed that vesicles produced at very high lipid concentrations exhibit size distributions and extent of multilamellar character comparable to systems produced at lower lipid levels.
Journal ArticleDOI

Sequence and specificity of two antibacterial proteins involved in insect immunity

TL;DR: It is believed that P9A and P9B play an important part in the humoral immune responses described previously and that the P9 proteins represent a new class of antibacterial agents for which the name cecropins is proposed.
Journal ArticleDOI

The co-evolution of host cationic antimicrobial peptides and microbial resistance

TL;DR: It is proposed that CAMPs and CAMP-resistance mechanisms have co-evolved, leading to a transient host–pathogen balance that has shaped the existing CAMP repertoire.
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