The role of tryptophan spatial arrangement for antimicrobial-derived, membrane-active peptidesadsorption and activity

Abstract

Herein we explored the role of topological distribution of aromatic amino acids in peptide–membrane interfacial interactions. The membrane activity of closely related peptides and their binding energy is sensitive to the positioning of minimum two tryptophans, and by the degree of flanking at the membrane interface mediated by aromatic amino acids.