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001-es BibID:	BIBFORM081485
Első szerző:	Di Natale, Giuseppe
Cím:	Cross-Talk Between the Octarepeat Domain and the Fifth Binding Site of Prion Protein Driven by the Interaction of Copper(II) with the N-terminus / Giuseppe Di Natale, Ildikó Turi, Giuseppe Pappalardo, Imre Sóvágó, Enrico Rizzarelli
Dátum:	2015
ISSN:	0947-6539 1521-3765
Megjegyzések:	Prion diseases are a group of neurodegenerative diseases based on the conformational conversion of the normal form of the prion protein (PrPC) to the disease?related scrapie isoform (PrPSc). Copper(II) coordination to PrPC has attracted considerable interest for almost 20?years, mainly due to the possibility that such an interaction would be an important event for the physiological function of PrPC. In this work, we report the copper(II) coordination features of the peptide fragment Ac(PEG11)3PrP(60?114) [Ac=acetyl] as a model for the whole N?terminus of the PrPC metal?binding domain. We studied the complexation properties of the peptide by means of potentiometric, UV/Vis, circular dichroism and electrospray ionisation mass spectrometry techniques. The results revealed that the preferred histidyl binding sites largely depend on the pH and copper(II)/peptide ratio. Formation of macrochelate species occurs up to a 2:1 metal/peptide ratio in the physiological pH range and simultaneously involves the histidyl residues present both inside and outside the octarepeat domain. However, at increased copper(II)/peptide ratios amide?bound species form, especially within the octarepeat domain. On the contrary, at basic pH the amide?bound species predominate at any copper/peptide ratio and are formed preferably with the binding sites of His96 and His111, which is similar to the metal?binding?affinity order observed in our previous studies.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk circular dichroism copper human prion protein mass spectrometry peptides
Megjelenés:	Chemistry-A European Journal. - 21 : 10 (2015), p. 4071-4084. -
További szerzők:	Turi Ildikó (1985-) (vegyész) Pappalardo, Giuseppe Sóvágó Imre (1946-) (vegyész) Rizzarelli, Enrico
Pályázati támogatás:	TAMOP-4.2.2A-11/1/KONV-2012-0043 TÁMOP
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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