Copper(II) binding to two novel histidine-containing model hexapeptides: evidence for a metal ion driven turn conformation(521 views) Di Natale G, Damante CA, Nagy Z, Osz K, Pappalardo G, Rizzarelli E, Sóvágó I
Keywords: Copper(ii), Histidine-Containing Peptides, Metal Complexes, Acetylglycylserylprolylhistidylalanylamide, Acetylhistidylprolylserylglycylhistidylalanylamide, Copper Complex, Cupric Ion, Glycine, Hexapeptide, Proline, Unclassified Drug, Amino Acid Sequence, Article, Circular Dichroism, Conformational Transition, Electron Spin Resonance, Metal Binding, Nuclear Magnetic Resonance, Ph Measurement, Potentiometry, Protein Analysis, Protein Folding, Protein Interaction, Protein Structure, Protein Synthesis, Stoichiometry, Ultraviolet Spectroscopy, Binding Sites, Electron Spin Resonance Spectroscopy, Magnetic Resonance Spectroscopy, Oligopeptides, Copper (ii),
Affiliations: *** IBB - CNR ***
Department of Chemical Sciences, University of Catania V.le A. Doria 6, 95125 Catania, Italy.
Department of Inorganic and Analytical Chemistry, University of Debrecen, 4010 Debrecen, Hungary
CNR Institute of Biostructures and Bioimaging, V.le A. Doria, 95125 Catania, Italy
References: Not available.
Copper(II) binding to two novel histidine-containing model hexapeptides: evidence for a metal ion driven turn conformation
The solution conformation and the copper(II) binding properties have comparatively been investigated for the two novel hexapeptides Ac-HPSGHA-NH(2) (P2) and Ac-HGSPHA-NH(2) (P4). The study has been carried out by means of CD, NMR, EPR and UV-Vis spectroscopic techniques in addition to potentiometric measurements to determine the stability constants of the different copper(II) complex species formed in the pH range 3-11. The peptides contain two histidine residues as anchor sites for the metal ion and differ only for the exchanged position of the proline residue with glycine. CD and NMR results for the uncomplexed peptide ligands suggest a predominantly unstructured peptide chain in aqueous solution. Potentiometric and spectroscopic data (UV-Vis, CD and EPR) show that both peptides strongly interact with copper(II) ions by forming complexes with identical stoichiometries but different structures. Furthermore, Far-UV CD experiments indicate that the conformation of the peptides is dramatically affected following copper(II) complexation with the P4 peptide adopting a beta-turn-like conformation.
Copper(II) binding to two novel histidine-containing model hexapeptides: evidence for a metal ion driven turn conformation
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Copper(II) binding to two novel histidine-containing model hexapeptides: evidence for a metal ion driven turn conformation
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(483 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