Abstract
We investigated how the interactions of membrane-active peptides with various types of membranes affect the secondary structures of these peptides. We chose two antimicrobial peptides, anoplin and W-MreB1-9, and one cell-penetrating peptide - (KFF)3K, which acts as a carrier of modified oligonucleotides to bacterial cells. First, we used circular dichroism (CD) spectroscopy to monitor peptide conformational changes in different membrane models: 1) micelles, single-layered detergents, charged SDS and zwitterionic DPC, 2) bilayered liposomes with compositions: POPC:POPG (3:1) and POPC:POPE (3:1); these liposomes have been designed to correspond to prokaryotic and eukaryotic membrane models, respectively, 3) lipolisaccharides (LPS) isolated from E.
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