Structural plasticity of the feline leukaemia virus fusion peptide

A circular dichroism study

Sarah M.A. Davies, Sharon M. Kelly, Nicholas C. Price, Jeremy P. Bradshaw

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The secondary structure of the feline leukaemia virus (FeLV) fusion peptide was investigated using circular dichroism (CD). Our results show that this peptide can readily flip between random, α-helical and β-sheet conformations, depending upon its environment. The CD spectrum changes from one characteristic of random coil to predominantly β-sheet type, and finally to that showing the characteristics of α-helical structure on moving from an aqueous solvent, through several increasingly hydrophobic systems, to a highly hydrophobic solvent. Electron microscopy confirmed the presence of β structure. We propose that the structural plasticity demonstrated here is crucial to the ability of the fusion peptide to perturb lipid bilayers, and thus promote membrane fusion.

Original languageEnglish
Pages (from-to)415-418
Number of pages4
JournalFEBS Letters
Volume425
Issue number3
DOIs
Publication statusPublished - 3 Apr 1998

Keywords

  • Circular dichroism
  • Electron microscopy
  • Feline leukemia virus
  • Fusion peptide
  • Spectrophotometry
  • Structural plasticity

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

Structural plasticity of the feline leukaemia virus fusion peptide : A circular dichroism study. / Davies, Sarah M.A.; Kelly, Sharon M.; Price, Nicholas C.; Bradshaw, Jeremy P.

In: FEBS Letters, Vol. 425, No. 3, 03.04.1998, p. 415-418.

Research output: Contribution to journalArticle

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