Simulation of the N-terminus of HIV-1 glycoprotein 41000 fusion peptide in micelles

Allison Langham, Yiannis Kaznessis

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


In this paper, the N-terminus of glycoprotein-41, the HIV-1 fusion peptide, was studied by molecular dynamics simulations in an explicit sodium dodecyl sulfate micelle. The simulation provides a detailed picture of the equilibrium structure and peptide stability as it interacts with the micelle. The equilibrium location of the peptide shows the peptide at the surface of the micelle with hydrophobic residues interacting with the micelle's core. At equilibrium, the peptide adopts an α-helical structure from residues 5-16 and a type-1 β-turn from 17-20 with the other residues exhibiting more flexible conformations. The primary hydrophobic interactions with the micelle are from the leucine and phenylalanine residues (Leu-7, Phe-8, Leu-9, Phe-11, Leu-12) while the alanine and glycine residues (Ala-1, Gly-3, Gly-5, Ala-6, Gly-10, Gly-13, Ala-14, Ala-15, Gly-16, Gly-10, Ala-21) interact favorably with water molecules. The results suggest that Phe-8, part of the highly conserved FLG motif of the fusion peptide, plays a key role in the interaction of the peptide with membranes. Our simulations corroborate experimental investigations of the fusion peptide in SDS micelles, providing a high-resolution picture that explains the experimental findings.

Original languageEnglish (US)
Pages (from-to)215-224
Number of pages10
JournalJournal of Peptide Science
Issue number4
StatePublished - Apr 2005


  • Fusion peptide
  • GP41
  • Membrane mimics
  • Micelles
  • Molecular dynamics simulation
  • Peptide membrane interactions
  • Sodium dodecyl sulfate


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