Keywords: Copper Complex, Copper Ion, Histidine, Ligand, Metal Ion, Nickel, Peptide Derivative, Absorption, Amino Terminal Sequence, Aqueous Solution, Article, Binding Site, Chemical Binding, Circular Dichroism, Electron Spin Resonance, Mass Spectrometry, Priority Journal, Stoichiometry,
Affiliations: *** IBB - CNR ***
Inst. Bio./Bio. sezione Catania CNR, V.Le A. Doria 6, 95125 Catania, Italy
Inst. Bio. /Bio. sezione Catania CNR, V. Le A. Doria 6, 95125 Catania, Italy
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Bonomo, R. P., Conte, E., Impellizzeri, G., Pappalardo, G., Purrello, R., Rizzarelli, E., (1996) J. Chem. Soc., Dalton Trans., p. 3093
Bonomo, R. P., Impellizzeri, G., Pappalardo, G., Purrello, R., Rizzarelli, E., Tabbi, G., (1998) J. Chem. Soc., Dalton Trans., p. 3851
Bonomo, R. P., Casella, L., De Gioia, L., Impellizzeri, G., Molinari, H., Jordan, T., Pappalardo, G., Rizzarelli, E., (1997) J. Chem. Soc., Dalton Trans., p. 2387
Chen, G. C., Yang, J. T., (1977) Anal. Lett., 10, p. 1195
Perczel, A., H llosi, M., (1996) Circular Dichroism and the Conformational Analysis of Biomolecules, p. 295. , ed. G. D. Fasman, Plenum, New York
W thrich, K., (1986) NMR of Proteins and Nucleic Acids, , Wiley, New York
W thrich, K., Billeter, M., Brown, W., (1984) J. Mol. Biol., 180, p. 715
Woody, R. W., (1974) Peptides, Polypeptides and Proteins, p. 338. , ed. E. R. Blout, F. A. Bovey, M. Goodman and L. Lotan, Wiley, New York
Manning, M. C., Illangasekare, M., Woody, R., (1988) Biophys. Chem., 31, p. 77
Tsangaris, J. M., Chang, J. W., Martin, R. B., (1969) J. Am. Chem. Soc., 91, p. 726
Fawcett, T. G., Bernarducci, E. E., Krough-Jespersen, K., Schugar, H. J., (1980) J. Am. Chem. Soc., 102, p. 2598
Bonomo, R. P., Cucinotta, V., D'Allessandro, F., Impellizzeri, G., Maccarrone, G., Vecchio, G., Rizzarelli, E., (1991) Inorg. Chem., 30, p. 2708
Pettit, L. D., Gregor, J. E., Kozlowsky, H., (1991) Perspectives on Bioinorganic Chemistry, 1, p. 1. , ed. R. W. Hay, J. R. Dilworth and K. B. Nolan, Jai Press, London
Varnagy, K., Szab, J., Sovago, I., Malandrinos, G., Hadjiliados, N., Sanna, D., Micera, G., (2000) J. Chem. Soc., Dalton Trans., p. 467
Martin, R. B., (1988) Metal Ions in Biological Systems, 1, p. 123. , ed. H. Sigel and A. Sigel, Marcel Dekker, New York
Pettit, L. D., Pyburn, S., Bal, W., Kozlowski, H., Bataille, M., (1990) J. Chem. Soc., Dalton Trans., p. 3565
Bryce, G. F., Roeske, R. W., Gurd, F. R. N., (1965) J. Biol. Chem., 240, p. 3837
Copper(II) and nickel(II) binding modes in a histidine-containing model dodecapeptide
The formation of complexes of HGGGHGHGGGHG (HG12) with copper(II) and nickel(II) have been studied in aqueous solution under various experimental conditions, including different pH and metal to ligand ratios. The study has been carried out using visible absorption, circular dichroism and electron paramagnetic resonance spectroscopic methods. Moreover, electrospray ionisation mass spectrometry has been used to directly determine the stoichiometry of the copper(II) complexes. The results indicate that HG12 can easily accommodate two metal ions in as many binding sites. The solution structure of the main complex species formed in the reaction of copper(II) with HG12 has been inferred by comparison with the copper(II) complexes formed with the shorter peptide fragments HGGGHG-NH2 (HG6), Ac-HGGGHG-NH2 (Ac-HG6) and Ac-HGGG-NH2 (AcHG4). With an equimolar metal to ligand ratio, the copper(II) ion binds preferentially in the N-terminal region of HG12. Conversely, Ni(II) ions form identical complexes regardless of whether the metal to ligand ratio is 1:1 or 2:1. Finally, the circular dichroism spectra indicate a significant modification of the peptide conformation upon metal binding.
Copper(II) and nickel(II) binding modes in a histidine-containing model dodecapeptide
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(357 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote