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.

@article{Qiang2009HIVFP,
  title={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.},
  author={Wei Qiang and David P Weliky},
  journal={Biochemistry},
  year={2009},
  volume={48 2},
  pages={289-301}
}
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… CONTINUE READING