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 language | English |
|---|---|
| Pages (from-to) | 415-418 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 425 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 3 Apr 1998 |
Funding
We wish to thank Mr S.R. Mitchell for expert technical assistance with the electron microscopy work, the Wellcome Trust for the award of a Prize Veterinary Research Training Scholarship to S.M.A.D., and the Biotechnology and Biological Sciences Research Council for provision of the CD facility.
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