The structure of a melittin-stabilized pore.

Abstract:

:Melittin has been reported to form toroidal pores under certain conditions, but the atomic-resolution structure of these pores is unknown. A 9-μs all-atom molecular-dynamics simulation starting from a closely packed transmembrane melittin tetramer in DMPC shows formation of a toroidal pore after 1 μs. The pore remains stable with a roughly constant radius for the rest of the simulation. Surprisingly, one or two melittin monomers frequently transition between transmembrane and surface states. All four peptides are largely helical. A simulation in a DMPC/DMPG membrane did not lead to a stable pore, consistent with the experimentally observed lower activity of melittin on anionic membranes. The picture that emerges from this work is rather close to the classical toroidal pore, but more dynamic with respect to the configuration of the peptides.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Leveritt JM 3rd,Pino-Angeles A,Lazaridis T

doi

10.1016/j.bpj.2015.04.006

subject

Has Abstract

pub_date

2015-05-19 00:00:00

pages

2424-2426

issue

10

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(15)00384-7

journal_volume

108

pub_type

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