The complex-formation equilibria of the pentadecapeptide TLEGTKKGHKLHLDY, the 114−128 protein fragment of SPARC, with the CuII ion have been investigated, at I = 0.1 mol·dm−3 (KNO3) and T = 298.2 K. Protonation and complexformation constants have been determined potentiometrically, and formation enthalpies measured by direct solution calorimetry; the complex-formation model and species stoichiometry have been carefully checked by means of UV/Vis absorption, CD and EPR spectroscopy. The structure hypotheses of the complex species are also based on detailed study of the 1H and 13C NMR spectra of the ligand in both the absence and presence of copper ions. The involvement in complex-formation of both the terminal amino and imidazole groups has been suggested and their specific behaviour at different pH values elucidated.
CuII ion coordination to an unprotected pentadecapeptide containing two His residues: competition between the terminal amino and the side-chain imidazole nitrogen donors
CONATO, Chiara;REMELLI, Maurizio;
2003
Abstract
The complex-formation equilibria of the pentadecapeptide TLEGTKKGHKLHLDY, the 114−128 protein fragment of SPARC, with the CuII ion have been investigated, at I = 0.1 mol·dm−3 (KNO3) and T = 298.2 K. Protonation and complexformation constants have been determined potentiometrically, and formation enthalpies measured by direct solution calorimetry; the complex-formation model and species stoichiometry have been carefully checked by means of UV/Vis absorption, CD and EPR spectroscopy. The structure hypotheses of the complex species are also based on detailed study of the 1H and 13C NMR spectra of the ligand in both the absence and presence of copper ions. The involvement in complex-formation of both the terminal amino and imidazole groups has been suggested and their specific behaviour at different pH values elucidated.I documenti in SFERA sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
