The reaction of the ruthenium(II) complex fac-[Ru(CO)(3)Cl(2)(N(1)-thz)] (I hereafter; thz = 1,3-thiazole) with human beta-amyloid peptide 1-28 (Abeta(28)) and the resulting {Ru(CO)(3)}(2+) peptide adduct was investigated by a variety of biophysical methods. (1)H NMR titrations highlighted a selective interaction of {Ru(CO)(3)}(2+) with Abeta(28) histidine residues; circular dichroism revealed the occurrence of a substantial conformational rearrangement of Abeta(28); electrospray ionization mass spectrometry (ESI-MS) suggested a prevalent 1:1 metal/peptide stoichiometry and disclosed the nature of peptide-bound metallic fragments. Notably, very similar ESI-MS results were obtained when I was reacted with Abeta(42). The implications of the above findings for a possible use of ruthenium compounds in Alzheimer's disease are discussed.

fac-Ru(CO)(3)(2+) selectively targets the histidine residues of the beta-amyloid peptide 1-28. Implications for new Alzheimer's disease treatments based on ruthenium complexes / D. Valensin; P. Anzini; E. Gaggelli; N. Gaggelli; G. Tamasi; R. Cini; C. Gabbiani; E. Michelucci; L. Messori; H. Kozlowski; G. Valensin. - In: INORGANIC CHEMISTRY. - ISSN 0020-1669. - STAMPA. - 49:(2010), pp. 4720-4722. [10.1021/ic902593e]

fac-Ru(CO)(3)(2+) selectively targets the histidine residues of the beta-amyloid peptide 1-28. Implications for new Alzheimer's disease treatments based on ruthenium complexes.

GABBIANI, CHIARA;MICHELUCCI, ELENA;MESSORI, LUIGI;
2010

Abstract

The reaction of the ruthenium(II) complex fac-[Ru(CO)(3)Cl(2)(N(1)-thz)] (I hereafter; thz = 1,3-thiazole) with human beta-amyloid peptide 1-28 (Abeta(28)) and the resulting {Ru(CO)(3)}(2+) peptide adduct was investigated by a variety of biophysical methods. (1)H NMR titrations highlighted a selective interaction of {Ru(CO)(3)}(2+) with Abeta(28) histidine residues; circular dichroism revealed the occurrence of a substantial conformational rearrangement of Abeta(28); electrospray ionization mass spectrometry (ESI-MS) suggested a prevalent 1:1 metal/peptide stoichiometry and disclosed the nature of peptide-bound metallic fragments. Notably, very similar ESI-MS results were obtained when I was reacted with Abeta(42). The implications of the above findings for a possible use of ruthenium compounds in Alzheimer's disease are discussed.
2010
49
4720
4722
D. Valensin; P. Anzini; E. Gaggelli; N. Gaggelli; G. Tamasi; R. Cini; C. Gabbiani; E. Michelucci; L. Messori; H. Kozlowski; G. Valensin
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/394191
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