Charged Antimicrobial Peptides Can Translocate across Membranes without Forming Channel-like Pores.

ABSTRACT: How can highly charged, cationic antimicrobial peptides (AMPs) translocate across hydrophobic lipid bilayers despite the prohibitive energetic penalty to do so? A common explanation has been the formation of peptide-lined channels. However, for most AMPs, no structures of membrane pores have been found despite clear evidence of membrane leakage and antimicrobial activity. The study here suggests an alternative and simple reason: for the AMP PGLa from Xenopus laevis (charge +5), such pores are not needed to explain both leakage and peptide translocation. Elevated-temperature multimicrosecond equilibrium simulations at all-atomistic level reveal that peptides spontaneously translocate across the membrane individually on a timescale of tens of microseconds, without forming pores. Both surface

SUBMITTER: Ulmschneider JP 

PROVIDER: S-EPMC5510918 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature