Describing the Mechanism of Antimicrobial Peptide Action with the Interfacial Activity Model

By William C. Wimley. ACS Chemical Biology, 2010

935 citations recorded by the source corpus.

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: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.

Subfields: Microbiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/eedebddbe66c5daef6d3732a35033270f99b929c

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In Microbiology

In Molecular Biology

Citations in the corpus

Antimicrobial Peptides: Diversity, Mechanism of Action and Strategies to Improve the Activity and Biocompatibility In Vivo (2018, background): “2 [39] and melittin [45,99] have been shown to form toroidal pores.”
Designing antimicrobial peptides: form follows function (2011, background): “Surrogate measures of bacterial killing, such as lipid vesicle experiment”