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Biomolecules, Volume 15, Issue 7
July 2025 - 149 articles
Cover Story: Short amphipathic peptides that disrupt lipid membranes can act as natural antimicrobial agents with therapeutic potential. Their efficacy in inducing membrane leakage depends on the properties of their amino acid sequence, which remain poorly understood. In the study presented herein, extended all-atom molecular dynamics simulations are combined with experimental leakage assays to examine the interactions of four peptides with anionic lipid membranes. Our findings demonstrate that water permeation depends on the type, length, and amphiphilicity of the peptides’ secondary structures, in addition to the hydropathy of their N- and C-termini. These insights will aid in the design of effective membrane-active peptides. View this paper
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Biomolecules - ISSN 2218-273X