Ac-PHGGGWGQ-NH2, an octarepeat peptide fragment of prion, is a relatively effective ligand for Cu2+ ions. At a pH of about 7.4 the major binding sites involve the imidazole nitrogen and two amide nitrogens of (3)Gly and (4)Gly giving a CuH-2L species. The stability of the complex formed is similar to other peptides having a similar type of coordination. The NMR spectra indicate that in CuH-2L the complex side chain of the Trp residue is located very close to the metal ion. The geometry around the Cu2+ ion seems to be slightly distorted from the tetragonal one. In strongly basic solution the coordination involves an additional amide nitrogen. In CuH-2L, CuH-3L and CuH-4L complexes the amide nitrogens involved in the metal ion binding are those placed towards the C-terminal from the His residue. The N-terminal of the unprotected octapeptide is very effective in binding the Cu2+ ion although at high pH the imidazole nitrogen may not be involved in metal ion binding.

Łuczkowski, M., Kozlowski, H., Stawikowski, M., Rolka, K., Gaggelli, E., Valensin, D., et al. (2002). Is the monomeric prion octapeptide repeat PHGGGWGQ a specific ligand for Cu2+ ions?. JOURNAL OF THE CHEMICAL SOCIETY. DALTON TRANSACTIONS, 11, 2269-2274 [10.1039/b201040m].

Is the monomeric prion octapeptide repeat PHGGGWGQ a specific ligand for Cu2+ ions?

GAGGELLI, ELENA;VALENSIN, DANIELA;VALENSIN, GIANNI
2002-01-01

Abstract

Ac-PHGGGWGQ-NH2, an octarepeat peptide fragment of prion, is a relatively effective ligand for Cu2+ ions. At a pH of about 7.4 the major binding sites involve the imidazole nitrogen and two amide nitrogens of (3)Gly and (4)Gly giving a CuH-2L species. The stability of the complex formed is similar to other peptides having a similar type of coordination. The NMR spectra indicate that in CuH-2L the complex side chain of the Trp residue is located very close to the metal ion. The geometry around the Cu2+ ion seems to be slightly distorted from the tetragonal one. In strongly basic solution the coordination involves an additional amide nitrogen. In CuH-2L, CuH-3L and CuH-4L complexes the amide nitrogens involved in the metal ion binding are those placed towards the C-terminal from the His residue. The N-terminal of the unprotected octapeptide is very effective in binding the Cu2+ ion although at high pH the imidazole nitrogen may not be involved in metal ion binding.
2002
Łuczkowski, M., Kozlowski, H., Stawikowski, M., Rolka, K., Gaggelli, E., Valensin, D., et al. (2002). Is the monomeric prion octapeptide repeat PHGGGWGQ a specific ligand for Cu2+ ions?. JOURNAL OF THE CHEMICAL SOCIETY. DALTON TRANSACTIONS, 11, 2269-2274 [10.1039/b201040m].
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/29124
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo