The influenza fusion peptide adopts a flexible flat V conformation in membranes.

Abstract:

:Knowledge about the influenza fusion peptide (FP) membrane insertion mode is crucial for understanding its fusogenic mechanism. NMR and electron paramagnetic resonance experiments showed that in micelles, the FP inserted as a fixed-angle inverted V. In membranes, however, it was shown to insert as a straight α-helix (by molecular-dynamics simulations) and to adopt multiple kinked conformations (by solid-state NMR). In this work we performed explicit-solvent molecular-dynamics simulations of the influenza FP, and its F9A and W14A mutants, in POPC membranes. The Hα1 chemical shifts predicted from the molecular-dynamics structures are in excellent agreement with the experimental values obtained for the three peptides. The peptide orientation and conformations observed from the simulations lead to a flexible flat-V model in which the peptide lies almost flat on the membrane surface and alternates between kinked and straight-helix conformations.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Légaré S,Lagüe P

doi

10.1016/j.bpj.2012.04.003

subject

Has Abstract

pub_date

2012-05-16 00:00:00

pages

2270-8

issue

10

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(12)00415-8

journal_volume

102

pub_type

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