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Copper(II) interaction with unstructured prion domain outside the octarepeat region: speciation, stability, and binding details of copper(II) complexes with prp106-126 peptides

Di Natale, Giuseppe and Grasso, Giulia and Impellizzeri, Giuseppe and La Mendola, Diego and Micera, Giovanni and Mihala, Nikolett and Nagy, Zoltán and Osz, Katalin and Pappalardo, Giuseppe and Rigó, Viktória and Rizzarelli, Enrico and Sanna, Daniele and Sóvágó, Imre (2005) Copper(II) interaction with unstructured prion domain outside the octarepeat region: speciation, stability, and binding details of copper(II) complexes with prp106-126 peptides. Inorganic Chemistry, Vol. 44 (20), p. 7214-7225. eISSN 1520-510X. Article.

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DOI: 10.1021/ic050754k

Abstract

Copper(II) complexes of the neurotoxic peptide fragments of human and chicken prion proteins were studied by potentiometric, UV−vis, CD, and EPR spectroscopic and ESI-MS methods. The peptides included the terminally blocked native and scrambled sequences of HuPrP106−126 (HuPrPAc106−126NH2 and ScrHuPrPAc106−126NH2) and also the nona- and tetrapeptide fragments of both the human and chicken prion proteins (HuPrPAc106−114NH2, ChPrPAc119−127NH2, HuPrPAc109−112NH2, and ChPrPAc122−125NH2). The histidyl imidazole-N donor atoms were found to be the major copper(II) binding sites of all peptides; 3N and 4N complexes containing additional 2 and 3 deprotonated amide-N donors, respectively, are the major species in the physiological pH range. The complex formation processes for nona- and tetrapeptides are very similar, supporting the fact that successive deprotonation and metal ion coordination of amide functions go toward the N-termini in the form of joined six- and five-membered chelates. As a consequence, the peptide sequences investigated here, related to the neurotoxic region of the human PrP106−126 sequence, show a higher metal-binding affinity than the octarepeat fragments. In the case of the HuPrP peptide sequences, a weak pH-dependent binding of the Met109 residue was also detected in the 3N-coordinated complexes.

Item Type:Article
ID Code:1451
Status:Published
Refereed:Yes
Uncontrolled Keywords:Copper(II) interaction, unstructured prion domain, peptides
Subjects:Area 03 - Scienze chimiche > CHIM/03 Chimica generale e inorganica
Divisions:001 Università di Sassari > 01 Dipartimenti > Chimica
002 Altri enti e centri di ricerca del Nord Sardegna > CNR-Consiglio Nazionale delle Ricerche > Istituto di chimica biomolecolare, Sassari
Publisher:American Chemical Society
eISSN:1520-510X
Deposited On:18 Aug 2009 10:05

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