Peptide–membrane interaction between targeting and lysis

Journal article

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.

Authors: Stutz, K; Kornmann, B; Müller, AT; Hiss, JA; Schneider, P

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: American Chemical Society
• Journal: ACS Chemical Biology
• Volume: 12
• Issue: 9
• Pages: 2254-2259
• Publication date: 2017-08-01
• Acceptance date: 2017-08-01
• DOI: 10.1021/acschembio.7b00504
• EISSN: 1554-8937
• ISSN: 1554-8929
• Pmid: 28763193
• Language: English
• Keywords: FFR