Subtle differences in initial membrane interactions underpin the selectivity of small antimicrobial peptides

Slavica Praporski, Adam Istvan Mechler, Frances Separovic, Lisandra Lorraine Martin

Research output: Contribution to journalArticleResearchpeer-review

10 Citations (Scopus)

Abstract

Host-secreted antimicrobial peptides (AMPs) are found in virtually all organisms, often providing innate immunity as the first line of defence against pathogens. Many AMPs kill pathogens by disrupting their cellular membranes and thus are similar to some antibiotic drugs. Likely drug candidate AMPs are found in non-mammalian hosts but are also haemolytic. Thus, it is crucial to understand the origins of membrane specificity and selectivity of the action of these AMPs. In this study, the membrane specificity of action of citropin 1.1, a 16-residue AMP, was studied by using a quartz crystal microbalance on the basis of mass and viscoelasticity changes in comparison to aurein 1.2 (13 residues) and maculatin 1.1 (21 residues). The membrane selectivity was largely reflected in the nature of the initial interaction of the peptide with the membrane. This initial interaction might determine whether the peptide transforms into a membrane-disrupting a-helical conformation and highlights subtle differences in the repositioning of this α-helical peptide in the membrane, as reflected by the viscoelasticity data, thus signifying the mechanistic pathway to membrane disruption
Original languageEnglish
Pages (from-to)91 - 96
Number of pages6
JournalChemPlusChem
Volume80
Issue number1
DOIs
Publication statusPublished - 2015

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