A molecular dynamics and circular dichroism study of a novel synthetic antimicrobial peptide

摘要

Antimicrobial peptides are a class of small, usually positively chargedamphiphilic peptides that are used by the innate immune system to combatbacterial infection in multicellular eukaryotes. Antimicrobial peptides areknown for their broad-spectrum antimicrobial activity and thus can be used as abasis for a development of new antibiotics against multidrug-resistantbacteria. The most challengeous task on the way to a therapeutic use ofantimicrobial peptides is a rational design of new peptides with enhancedactivity and reduced toxicity. Here we report a molecular dynamics and circulardichroism study of a novel synthetic antimicrobial peptide D51. This peptidewas earlier designed by Loose et al. using a linguistic model of naturalantimicrobial peptides. Molecular dynamics simulation of the peptide folding inexplicit solvent shows fast formation of two antiparallel beta strandsconnected by a beta-turn that is confirmed by circular dichroism measurements.Obtained from simulation amphipatic conformation of the peptide is analysed andpossible mechanism of its interaction with bacterial membranes together withways to enhance its antibacterial activity are suggested.