UNSPECIFIED. (2002) Binding of prion protein to lipid membranes and implications for prion conversion. Journal of Molecular Biology, 315 (5). pp. 1241-1256. ISSN 0022-2836

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Abstract

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
ISSN:	0022-2836
Date:	1 February 2002
Volume:	315
Number:	5
Number of Pages:	16
Page Range:	pp. 1241-1256
Identification Number:	10.1006/jmbi.2001.5322
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/11245

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