Determination of the HIV-1 gp41 fusogenic core conformation modeled by synthetic peptides: applicable for identification of HIV-1 fusion inhibitors

Peptides. 2003 Sep;24(9):1303-13. doi: 10.1016/j.peptides.2003.07.013.


Triggered by receptor binding of gp120, the human immunodeficiency virus type 1 (HIV-1) gp41 changes its conformation to a fusogenic six-helix bundle structure. In the present study, this core conformation modeled by the peptides derived from the gp41 N- and C-terminal heptad repeat regions was determined by fluorescence native polyacrylamide gel electrophoresis and size exclusion high-performance liquid chromatography (HPLC). Two previously described small molecule HIV-1 fusion inhibitors significantly blocked the six-helix bundle formation. It suggests that these biophysical techniques can be used in a novel way to study the conformational change of gp41 during virus entry into cells and to identify HIV-1 fusion inhibitors.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Drug Evaluation, Preclinical*
  • Electrophoresis, Polyacrylamide Gel
  • HIV Envelope Protein gp41 / chemistry*
  • HIV Fusion Inhibitors / chemistry*
  • HIV Fusion Inhibitors / pharmacology*
  • HIV-1 / chemistry*
  • Models, Molecular
  • Molecular Conformation
  • Molecular Sequence Data
  • Peptide Library
  • Protein Structure, Secondary


  • HIV Envelope Protein gp41
  • HIV Fusion Inhibitors
  • Peptide Library