Abstract
Infections by drug-resistant bacteria pose a growing threat to human health, so developing new antimicrobial drugs is becoming an increasingly urgent requirement. Antimicrobial peptides are an important part of the innate immune system of many organisms, which have a broad spectrum of antimicrobial activity and little likelihood to trigger resistance, so they are considered good candidates for developing new antimicrobial drugs. In this paper, the interaction of indolicidin (IR13) and its derived peptides CP10A, CP-11 and cycloCP-11 with Gram-negative bacterial model membranes is investigated using coarse-grained molecular dynamics approach. The aim is to analyse the behaviour of these antimicrobial peptides when interacting with Gram-negative bacterial membranes. The widely studied phospholipid bilayer consisting of POPC and POPG is used as a Gram-negative bacterial membrane model in the simulations. The results show that the derived peptides CP-11 and cycloCP-11 are more active against Gram-negative bacteria than IR13 and CP10A. The dynamic behaviour of the four antimicrobial peptides on the membrane is different, and the peptide-membrane interactions induce changes in the thickness and surface area of the phospholipid bilayer, diminish membrane mobility, and so on. The present study provides important insights into the mechanism of interaction between antimicrobial peptides and phospholipid membranes by analysing them at the molecular level, and is therefore informative for designing new derivative peptides.
Published Version
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