The mechanism by which amphipathic peptides permeabilize biological membranes is poorly understood. Do the peptides form well-defined pores or simply dissolve the membranes in a detergent-like fashion? What is the lifetime of these pores? How do the sequence and structure of these peptides determine their permeabilizing function? Both experiment and theory face formidable challenges in obtaining detailed information on such labile structures. Over the last few years we have carried out multi-microsecond, all-atom molecular dynamics simulations of lipid bilayers with inserted peptide oligomers. Such simulations of melittin, magainin, PGLa, alamethicin, protegrin, as well as novel peptides designed by the Wimley and Hristova groups have provided useful insights into the sequence determinants of pore-forming ability.<br/>

Membrane pore formation by antimicrobial, lytic, and designed peptides

2019 Spring National Meeting

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