fac-{Ru(CO)3}2+ Selectively Targets the Histidine Residues of the β-Amyloid Peptide 1-28. Implications for New Alzheimer's Disease Treatments Based on Ruthenium Compl

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• 作者：Daniela Valensin ; Paolo Anzini ; Elena Gaggelli ; Nicola Gaggelli ; Gabriella Tamasi ; Renzo Cini ; Chiara Gabbiani ; Elena Michelucci ; Luigi Messori ; Henryk Kozlowski ; Gianni Valensin
• 刊名：Inorganic Chemistry
• 出版年：2010
• 出版时间：June 7, 2010
• 年：2010
• 卷：49
• 期：11
• 页码：4720-4722
• 全文大小：693K
• 年卷期：v.49,no.11(June 7, 2010)
• ISSN：1520-510X

文摘

The reaction of the ruthenium(II) complex fac-[Ru(CO)₃Cl₂(N¹-thz)] (I hereafter; thz = 1,3-thiazole) with human β-amyloid peptide 1-28 (Aβ₂₈) and the resulting {Ru(CO)₃}²⁺ peptide adduct was investigated by a variety of biophysical methods. ¹H NMR titrations highlighted a selective interaction of {Ru(CO)₃}²⁺ with Aβ₂₈ histidine residues; circular dichroism revealed the occurrence of a substantial conformational rearrangement of Aβ₂₈; 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 Aβ₄₂. The implications of the above findings for a possible use of ruthenium compounds in Alzheimer’s disease are discussed.