The fusion peptide of simian immunodeficiency virus and the phase behaviour of N-methylated dioleoylphosphatidylethanolamine

Thad A. Harroun, Kia Balali-Mood, Ian Gourlay, Jeremy P. Bradshaw

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Temperature-scan X-ray scattering was used to study the effect of the fusion peptide of simian immunodeficiency virus (SIV) on the lipid polymorphism of N-methylated dioleoylphosphatidylethanolamine (DOPE-Me), in the presence and absence of one or both of the fusion inhibitors carbobenzoxy-D-phenylalanine-L- phenylalanine-glycine and 1-lauroyl-2-hydroxy-sn-glycero-3-phosphocholine (LPC). Using X-ray diffraction at stations 2.1 and 8.2 of the Synchrotron Radiation Source at Daresbury Laboratory, UK, the structure of multilamellar vesicles (MLVs) was probed as the temperature was raised from 20 to 90 °C. The results are compared to those of similar studies, reported earlier, that used the fusion peptide of feline leukaemia virus (FeLV) which, at 28 amino acid residues in length, is considerably longer than the SIV peptide (12 amino acid residues). We interpret the results within the framework of current understanding of membrane fusion, and demonstrate how observed lipid polymorphism might describe the fusion process.

Original languageEnglish
Pages (from-to)62-68
Number of pages7
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1617
Issue number1-2
DOIs
Publication statusPublished - 31 Oct 2003

Keywords

  • Biomembrane fusion
  • Cubic phase
  • Hexagonal phase
  • Inhibitor
  • Lamellar phase
  • Small angle X-ray diffraction

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

Fingerprint Dive into the research topics of 'The fusion peptide of simian immunodeficiency virus and the phase behaviour of N-methylated dioleoylphosphatidylethanolamine'. Together they form a unique fingerprint.

Cite this