Copper(II) binding modes in the prion octapeptide PHGGGWGQ: A spectroscopic and voltammetric study(408 views visite) Bonomo RP, Imperllizzeri G, Pappalardo G, Rizzarelli E, Tabbì G
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2000 Nov 17; 6(22): 4195-4202.
Keywords Parole chiave: Circular Dichroism, Copper, Cyclic Voltammetry, Epr Spectroscopy, Peptides, Prion, Copper Ion, Octapeptide, Oligopeptide, Prion Protein, Absorption Spectroscopy, Amino Acid Sequence, Article, Chemical Analysis, Chemical Structure, Complex Formation, Electrochemistry, Electron Spin Resonance, Human, Nonhuman, Potentiometry, Electron Spin Resonance Spectroscopy, Molecular Structure,
Affiliations Affiliazioni: Dipartimento di Scienze Chimiche, Università di Catania, V.Le A. Doria 6, 95125 Catania, Italy Ist. Stud. Sostanze Naturali I., Sezione Stud. Modelli Metallo E., V.Le A. Doria 6, 95125 Catania, Italy
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http: //www. lem. ch. unito. it/chemistry/electrochemistry. html, Copyright by Professor Carlo Nervi, this package can be downloaded at the internet addressBard, A. J., (1980) Electrochemical Methods: Fundamentals and Applications, p. 430. , Wiley
Sawyer, D. T., Roberts, J. L., (1974) Experimental Electrochemistry for Chemists, p. 42. , Wiley
Copper(II) binding modes in the prion octapeptide PHGGGWGQ: A spectroscopic and voltammetric study
The N-terminal octapeptide repeat region of human prion protein (PrPc) is known to bind CuII. To investigate the binding modes of copper in PrPc, an octapeptide Ac-PHGGGWGQ-NH2 (1), which corresponds to an octarepeat sequence, and a tetrapeptide Ac-HGGG-NH2 (2) have been synthesised. The copper(II) complexes formed with 1 and 2 have been studied by circular dichroism (CD) and electron spin resonance (ESR) spectroscopy. Both peptides form 1:1 complexes with CuII at neutral and basic pH. CD, ESR and visible absorption spectra suggest a similar co-ordination sphere of the metal ion in both peptides, which at neutral pH consists of a square pyramidal geometry with three peptidic nitrogens and the imidazole nitrogen as donor atoms. Cyclic voltammetric measurements were used to confirm the geometrical features of these copper(II) complexes: the observation of negative redox potentials are in good agreement with the inferred geometry. All these results taken together suggest that peptide 1 provides a single metal binding site to which copper(II) binds strongly at neutral and basic pH and that the binding of the metal induces the formation of a stiffened structure in the HGGG peptide fragment.
Copper(II) binding modes in the prion octapeptide PHGGGWGQ: A spectroscopic and voltammetric study
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(371 visite) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 DettagliEsporta in BibTeXEsporta in EndNote
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