Binding of prion protein to lipid membranes and implications for prion conversion
UNSPECIFIED. (2002) Binding of prion protein to lipid membranes and implications for prion conversion. Journal of Molecular Biology, 315 (5). pp. 1241-1256. ISSN 0022-2836Full text not available from this repository.
Official URL: http://dx.doi.org/10.1006/jmbi.2001.5322
The binding of the Syrian hamster prion protein, SHaPrP(90-231), to model lipid membranes was investigated by tryptophan fluorescence. Membranes composed of negatively charged or zwitterionic lipids, and raft-like membranes containing dipalmitoylphosphatidylcholine1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), cholesterol and sphingomyelin, were investigated. It was found that SHaPrP(90-231) binds to negatively charged lipid membranes and raft-like membranes. Binding of PrP to negatively charged lipid membranes involves both electrostatic and hydrophobic lipid-protein interactions and results in partial insertion of PrP into the lipid bilayer. This membrane-inserted conformation of PrP is richer in beta-sheet structure and has a disruptive effect on the integrity of the lipid bilayer, leading to total release of vesicle contents. In contrast, the binding of PrP to raft-like membranes is driven by hydrophobic lipid-protein interactions and induces the formation of alpha-helical structure. This conformation of PrP with a high content of alpha-helix is formed only at pH 7 and does not destabilize the lipid bilayer. Our findings support the view that an interaction of PrP with lipid membranes could play a role in PrP conversion. (C) 2002 Elsevier Science Ltd.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||Journal of Molecular Biology|
|Publisher:||ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD|
|Date:||1 February 2002|
|Number of Pages:||16|
|Page Range:||pp. 1241-1256|
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