HIV fusion peptide and its cross-linked oligomers: efficient syntheses, significance of the trimer in fusion activity, correlation of beta strand conformation with membrane cholesterol, and proximity to lipid headgroups.

ABSTRACT: For enveloped viruses such as HIV, an approximately 20-residue N-terminal fusion peptide domain in the envelope protein binds to target cell membranes and plays a key role in fusion between the viral and cellular membranes during infection. The chemically synthesized HIV fusion peptide (HFP) catalyzes fusion between membrane vesicles and is a useful model system for understanding some aspects of HIV fusion. Previous studies have shown a common trimeric state for the envelope protein from several different viruses, including HIV, and in this study, practical high-yield syntheses are reported for HFP monomer (HFPmn) and chemically cross-linked HFP dimer (HFPdm), trimer (HFPtr), and tetramer (HFPte). The vesicle fusion rates per strand were ordered as follows: HFPmn < HFPdm < HFPtr approximat

SUBMITTER: Qiang W 

PROVIDER: S-EPMC2680607 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature