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pubmed-article:11827491pubmed:abstractTextThe 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 dipalmitoylphosphatidylcholine(1,2-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.lld:pubmed
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pubmed-article:11827491pubmed:copyrightInfoCopyright 2002 Elsevier Science Ltd.lld:pubmed
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pubmed-article:11827491pubmed:dateRevised2010-11-18lld:pubmed
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pubmed-article:11827491pubmed:articleTitleBinding of prion protein to lipid membranes and implications for prion conversion.lld:pubmed
pubmed-article:11827491pubmed:affiliationDepartment of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.lld:pubmed
pubmed-article:11827491pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11827491pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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