pubmed-article:11827491 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11827491 | lifeskim:mentions | umls-concept:C0033164 | lld:lifeskim |
pubmed-article:11827491 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
pubmed-article:11827491 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
pubmed-article:11827491 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:11827491 | lifeskim:mentions | umls-concept:C0439836 | lld:lifeskim |
pubmed-article:11827491 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:11827491 | pubmed:dateCreated | 2002-2-5 | lld:pubmed |
pubmed-article:11827491 | pubmed:abstractText | 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 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 |
pubmed-article:11827491 | pubmed:language | eng | lld:pubmed |
pubmed-article:11827491 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11827491 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11827491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11827491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11827491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11827491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11827491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11827491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11827491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11827491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11827491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11827491 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11827491 | pubmed:month | Feb | lld:pubmed |
pubmed-article:11827491 | pubmed:issn | 0022-2836 | lld:pubmed |
pubmed-article:11827491 | pubmed:author | pubmed-author:SangheraNarin... | lld:pubmed |
pubmed-article:11827491 | pubmed:author | pubmed-author:PinheiroTeres... | lld:pubmed |
pubmed-article:11827491 | pubmed:copyrightInfo | Copyright 2002 Elsevier Science Ltd. | lld:pubmed |
pubmed-article:11827491 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11827491 | pubmed:day | 1 | lld:pubmed |
pubmed-article:11827491 | pubmed:volume | 315 | lld:pubmed |
pubmed-article:11827491 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11827491 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11827491 | pubmed:pagination | 1241-56 | lld:pubmed |
pubmed-article:11827491 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:11827491 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:11827491 | pubmed:articleTitle | Binding of prion protein to lipid membranes and implications for prion conversion. | lld:pubmed |
pubmed-article:11827491 | pubmed:affiliation | Department of Biological Sciences, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK. | lld:pubmed |
pubmed-article:11827491 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11827491 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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