Inhibition of HIV-1 infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein GP41

Biochem Biophys Res Commun. 1993 Sep 15;195(2):533-8. doi: 10.1006/bbrc.1993.2078.

Abstract

A synthetic peptide, corresponding to the sequence (637-666) of the HIV-1 glycoprotein gp41, inhibited the replication of an array of HIV-1 strains. The peptide (637-666) selectively binds to the fusion domain at the N-terminus of gp41, suggesting that inhibition of HIV-1 infection is caused by blocking fusion of HIV-1 with cells or of infected cells with uninfected cells. Since this peptide has antiviral activity against both homologous and heterologous HIV-1 isolates and has no detectable cytotoxicity, it offers a novel approach to chemotherapy and prophylaxis of AIDS.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cell Line
  • Gene Products, env / metabolism
  • HIV Envelope Protein gp160
  • HIV Envelope Protein gp41 / metabolism*
  • HIV-1 / drug effects
  • HIV-1 / metabolism
  • HIV-1 / physiology*
  • Humans
  • Immune Sera / pharmacology
  • Molecular Sequence Data
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / metabolism
  • Peptide Fragments / pharmacology*
  • Peptides / chemical synthesis
  • Peptides / metabolism
  • Peptides / pharmacology*
  • Protein Precursors / metabolism
  • Virus Replication / drug effects*

Substances

  • Gene Products, env
  • HIV Envelope Protein gp160
  • HIV Envelope Protein gp41
  • Immune Sera
  • Peptide Fragments
  • Peptides
  • Protein Precursors