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Publication Abstract from PubMed

Certain cationic peptides interact with biological membranes. These often-complex interactions can result in peptide targeting to the membrane, or in membrane permeation, rupture, and cell lysis. We investigated the relationship between the structural features of membrane-active peptides and these effects, to better understand these processes. To this end, we employed a computational method for morphing a membranolytic antimicrobial peptide into a nonmembranolytic mitochondrial targeting peptide by "directed simulated evolution." The results obtained demonstrate that superficially subtle sequence modifications can strongly affect the peptides' membranolytic and membrane-targeting abilities. Spectroscopic and computational analyses suggest that N- and C-terminal structural flexibility plays a crucial role in determining the mode of peptide-membrane interaction.

Peptide-Membrane Interaction between Targeting and Lysis.,Stutz K, Muller AT, Hiss JA, Schneider P, Blatter M, Pfeiffer B, Posselt G, Kanfer G, Kornmann B, Wrede P, Altmann KH, Wessler S, Schneider G ACS Chem Biol. 2017 Aug 8. doi: 10.1021/acschembio.7b00504. PMID:28763193^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.