Premium
Structure and function of membrane fusion peptides
Author(s) -
Tamm Lukas K.,
Han Xing,
Li Yinling,
Lai Alex L.
Publication year - 2002
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10261
Subject(s) - lipid bilayer fusion , chemistry , membrane , fusion , hemagglutinin (influenza) , peptide , fusion mechanism , biophysics , membrane protein , function (biology) , biochemistry , microbiology and biotechnology , biology , philosophy , linguistics , gene
Membrane fusion peptides are highly conserved hydrophobic domains of fusion proteins that insert into membranes during membrane fusion. Recent success with solving the structures of the influenza hemagglutinin fusion peptide and some critical mutants of this peptide in membrane environments at high resolution has led to a new understanding of the mechanism of membrane fusion. This review highlights the structures that have been solved and summarizes recent thermodynamic and spectroscopic studies on the interactions of this interesting class of peptides with lipid bilayers. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 66: 249–260, 2002