Oblique membrane insertion of viral fusion peptide probed by neutron diffraction

Jeremy P. Bradshaw, Malcolm J.M. Darkes, Thad A. Harroun, John Katsaras, Richard M. Epand

Research output: Contribution to journalArticle

91 Citations (Scopus)

Abstract

Fusion peptides mimic the membrane fusion activities of the larger viral proteins from which they derive their sequences. A possible mode of activity involves their oblique insertion into lipid bilayers, causing membrane disruption by promoting highly curved hemifusion intermediates, leading to fusion. We have determined the location and orientation of the simian immunodeficiency virus (SIV) fusion peptide in planar lipid bilayers using neutron lamellar diffraction. The helical axis of the peptide adopts an angle of 55°relative to the membrane normal, while it positions itself nearest the lipid bilayer surface. This is the first direct observation of the structural interaction between a fusion peptide and a phospholipid bilayer.

Original languageEnglish
Pages (from-to)6581-6585
Number of pages5
JournalBiochemistry
Volume39
Issue number22
DOIs
Publication statusPublished - 6 Jun 2000

ASJC Scopus subject areas

  • Biochemistry

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