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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)
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- 2007-01-01T00:00:00+01:00 (literal)
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- 10.1016/j.ica.2007.05.026 (literal)
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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)
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- 1-Guantieri V., 2-Venzo A., 3-Di Marco V.B., 1-Acampora M., 4-Biondi B. (literal)
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- 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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