Plasticity of influenza haemagglutinin fusion peptides and their interaction with lipid bilayers.

ABSTRACT: A detailed molecular dynamics study of the haemagglutinin fusion peptide (N-terminal 20 residues of the HA2 subunits) in a model bilayer has yielded useful information about the molecular interactions leading to insertion into the lipids. Simulations were performed on the native sequence, as well as a number of mutant sequences, which are either fusogenic or nonfusogenic. For the native sequence and fusogenic mutants, the N-terminal 11 residues of the fusion peptides are helical and insert with a tilt angle of approximately 30 degrees with respect to the membrane normal, in very good agreement with experimental data. The tilted insertion of the native sequence peptide leads to membrane bilayer thinning and the calculated order parameters show larger disorder of the alkyl chains. These resu

SUBMITTER: Vaccaro L 

PROVIDER: S-EPMC1305003 | biostudies-literature | 2005 Jan

REPOSITORIES: biostudies-literature