title: Viral fusion peptides: a tool set to disrupt and connect biological membranes.
abstract: The structure and function of viral fusion peptides are reviewed. The fusion peptides of influenza virus hemagglutinin and human immunodeficiency virus are used as paradigms. Fusion peptides associated with lipid bilayers are conformationally polymorphic. Current evidence suggests that the fusion-promoting state is the obliquely inserted alpha-helix. Fusion peptides also have a tendency to self-associate into beta-sheets at membrane surfaces. Although the conformational conversion between alpha- and beta-states is reversible under controlled conditions, its physiological relevance is not yet known. The energetics of peptide insertion and self-association could be measured recently using more soluble "second generation" fusion peptides. Fusion peptides have been reported to change membrane curvature and the state of hydration of membrane surfaces. The combined results are built into a model for the mechanism by which fusion peptides are proposed to assist in biological membrane fusion.
authors: Department of Molecular Physiology and Biological Physics and Center for Structural Biology, University of Virginia Health Sciences Center, Charlottesville 22908-0736, USA. lkt2e@virginia.edu
authors: L K
authors: LK
authors: Tamm
authors: X
authors: X
authors: Han
mesh_terms: D000595:Amino Acid Sequence; D008561:Membrane Fusion / Q000502:physiology*; D008969:Molecular Sequence Data; D014760:Viral Fusion Proteins / Q000737:chemistry / Q000502:physiology*
chemical_list: D014760:Viral Fusion Proteins