Abstract
The effects of two fusion inhibitors on the lipid polymorphism of N-methylated dioleoylphosphatidylethanolamine were studied using temperature-resolved, small-angle X-ray diffraction. The inhibitory role of the tri-peptide carbobenzoxy-D-phenylalanine-L-phenylalanine-glycine and the lipid 1-lauroyl-2-hydroxy-sn-glycero-3-phosphocholine in the fusion pathway was studied, using the non-lamellar phase behaviour of the lipid as a model. We used p15EK, the N-terminal region of gp41 from feline leukaemia virus as promoter of membrane fusion, and measured the structural parameters of each observed lipid phase as a function of temperature. The fusion inhibitors were found to impede the expression of negative curvature of lipid monolayers even in the presence of fusion peptide. The results of this study are interpreted in relation to models of the membrane fusion mechanism.
| Original language | English |
|---|---|
| Pages (from-to) | 119-128 |
| Number of pages | 10 |
| Journal | Biochimica et Biophysica Acta - Biomembranes |
| Volume | 1561 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 19 Mar 2002 |
Funding
Grateful thanks are extended to Dr Heinz Amenitsch at Sincrotrone Trieste Elettra and Dr Gunter Grossman at Daresbury SRS for their expert technical assistance, and Ms S. Darkes for commenting on the manuscript. This work was supported by grants from the Wellcome Trust, the Central Laboratories of the Research Councils (CLRC) and the European Community HPP-TAMRI Program.
Keywords
- Biomembrane fusion
- Cubic phase
- Hexagonal phase
- Inhibitor
- Lamellar phase
- Small angle X-ray diffraction
- Small angle X-ray scattering
- Time resolved X-ray diffraction
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Cell Biology