Potentiometric and NMR studies on Cd2+ coordination with the histidine-containing Ac184-188NH2 prion protein fragment (Articolo in rivista)

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  • Potentiometric and NMR studies on Cd2+ coordination with the histidine-containing Ac184-188NH2 prion protein fragment (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.ica.2007.05.026 (literal)
Alternative label
  • 1-Guantieri V., 2-Venzo A., 3-Di Marco V.B., 1-Acampora M., 4-Biondi B. (2007)
    Potentiometric and NMR studies on Cd2+ coordination with the histidine-containing Ac184-188NH2 prion protein fragment
    in Inorganica Chimica Acta (Testo stamp.); Elsevier BV, Amsterdam (Paesi Bassi)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • 1-Guantieri V., 2-Venzo A., 3-Di Marco V.B., 1-Acampora M., 4-Biondi B. (literal)
Pagina inizio
  • 4051 (literal)
Pagina fine
  • 4057 (literal)
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  • http://www.elsevier.com/locate/ica (literal)
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  • 360 (literal)
Rivista
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  • 7 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1-Dipartimento di Scienze Chimiche, Via Marzolo 1, 35131 Padova, Italy 2-CNR-ISTM, Via Marzolo 1, 35131 Padova, Italy 3-CNR, Istituto di Chimica Biomolecolare, Via Marzolo 1, 35131 Padova, Italy (literal)
Titolo
  • Potentiometric and NMR studies on Cd2+ coordination with the histidine-containing Ac184-188NH2 prion protein fragment (literal)
Abstract
  • To elucidate the specific mode and site of binding between metal ions and prion protein (PrPc), we synthesized the pentapeptide Ac184-188NH2 (AcIKQHTNH2), corresponding to helical region II of the protein, and its analogous acetylated at the lysine side chain. The acid-base properties of both peptides and their interaction with Cd2+ were studied in aqueous solution by NMR and potentiometry. Speciation data were compared with those achieved for Cd2+/4-methylimidazole, taken as the reference system. Both NMR and potentiometric data indicate that Cd2+ is coordinated by the histidine residue. The involvement of the side chain amine of lysine in the metal coordination is excluded by NMR data, whereas a role for either the carbonyl or the amide group of threonine is suggested. (literal)
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