Membrane de stabilization induced by the human immunodeficiency virus type-1 fusion peptide

José L. Nieva*, Félix M. Goñi, Arruro Muga, Shlomo Nir, Francisca Pereira

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The human immunodeficiency virus type-1 (HIV-1) fusion peptide, corresponding to a sequence of 23 amino acid residues at the N-terminus of the spike transmembrane subunit gp41, has the capacity to destabilize negatively charged and neutral large unilamellar vesicles, representing, respectively, the acidic and the neutral fraction of the plasma membrane lipids of viral target cells. As revealed by infrared spectroscopy, the peptide associated with the vesicles may exist in different conformations. In negatively charged membranes the structure is mainly an α-helix, while in Ca2+-neutralized negatively charged membranes the conformation switches to a predominantly extended conformation. In membranes composed of zwitterionic phospholipids and cholesterol, the peptide also adopts a predominant extended structure. The α-helical structure permeabilizes negatively charged vesicles but does not induce membrane fusion. The peptide in β-type conformation, on the other hand, permeabilizes neutral membranes and triggers fusion. As seen by 31P NMR, the latter structure also exhibits the capacity to alter the lamellar organization of the membrane.

Original languageEnglish
Pages (from-to)365-369
Number of pages5
JournalInternational Journal of Peptide Research and Therapeutics
Volume4
Issue number4-6
DOIs
StatePublished - 1997

Keywords

  • Conformational switching
  • Membrane fusion
  • Peptide conformation
  • Peptide-lipid interaction

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