Influence of Acyl Chain Saturation on the Membrane-Binding Activity of a Short Antimicrobial Peptide.

ABSTRACT: Different bacterial types and their living environments can lead to different saturations in the chains of their membrane lipids. Such structural differences may influence the efficacy of antibiotics that target bacterial membranes. In this work, the effects of acyl chain saturation on the binding of an antimicrobial peptide G₄ have been examined as a function of the packing density of lipid monolayers by combining external reflection Fourier transform infrared (ER-FTIR) spectroscopy and neutron reflection (NR) measurements. Langmuir monolayers were formed from 1,2-dipalmitoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (DPPG) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-(1'-rac-glycerol) (POPG), respectively, with the initial surface pressures controlled

SUBMITTER: Ciumac D 

PROVIDER: S-EPMC6044940 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature