Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5504
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dc.contributor.authorGralka, Een_us
dc.contributor.authorValensin, Danielaen_us
dc.contributor.authorPorciatti, Een_us
dc.contributor.authorGajda, Cen_us
dc.contributor.authorGaggelli, Elenaen_us
dc.contributor.authorValensin, Giannien_us
dc.contributor.authorKamysz, Wen_us
dc.contributor.authorNadolny, Ren_us
dc.contributor.authorGuerrini, Ren_us
dc.contributor.authorBacco, Den_us
dc.contributor.authorRemelli, Men_us
dc.contributor.authorKozlowski, H.en_us
dc.date.accessioned2021-03-30T15:52:11Z-
dc.date.available2021-03-30T15:52:11Z-
dc.date.issued2008-
dc.identifier.issn1477-9226en_US
dc.identifier.urihttp://hdl.handle.net/20.500.12779/5504-
dc.description35684en_US
dc.description.abstractThe prion protein (PrP) is a Cu2+-binding cell-surface glycoprotein. Using PrP peptide fragments, by means of potentiometric, spectroscopic and thermodynamic techniques, we have shown that Cu2+ ions bind to the region comprising His-96, His-111 and the octarepeat domain within residues 60–91. Cu2+ may bind in different modes, which strongly depend both on His position within the peptide sequence and on the adjacent residues. We have used a series of protected oligopeptides having His at the C- or the N-terminus, inducing different binding modes to amide nitrogens around the His residue, either towards the N- or C-terminus. His imidazole acts as an anchoring site for Cu2+ and then binding to ionized amide nitrogens follows. When it is directed towards the C-terminus the formation of a less stable seven-membered chelate ring with a {Nim, N-} binding mode occurs. When coordination goes towards the N-terminus the thermodynamically more stable six-membered chelate ring is formed. NMR data suggest that both the coordination modes are possible for the model peptides; however, the thermodynamic measurements show that they only slightly differ in energy and the influence of the adjacent amino acid residues can address the coordination toward the C- or the N-terminus.en_US
dc.language.isoenen_US
dc.relationNoneen_US
dc.relation.ispartofDALTON TRANSACTIONSen_US
dc.titleCuII binding sites located at His-96 and His-111 of the human prion protein: thermodynamic and spectroscopic studies on model peptidesen_US
dc.typeArticleen_US
dc.identifier.doi10.1039/b806192ken_US
dc.identifier.scopus2-s2.0-52349102890en_US
dc.identifier.isiWOS:000259411500014en_US
dc.relation.volume38en_US
dc.description.firstpage5207en_US
dc.description.lastpage5219en_US
dc.description.thirdmissionNot applicableen_US
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeArticle-
item.fulltextNo Fulltext-
crisitem.author.orcid0000-0003-4187-3919-
crisitem.author.orcid9810-
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