Department of Chemistry, University of Siena, Via A. Moro, 53100 Siena, Italy.
Inorg Chem. 2010 Jun 7;49(11):4720-2. doi: 10.1021/ic902593e.
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.
钌（II）配合物 fac-[Ru(CO)(3)Cl(2)(N(1)-thz)]（以下简称 I；thz = 1,3-噻唑）与人类β-淀粉样肽 1-28（Abeta(28)）的反应以及由此产生的{Ru(CO)(3)}(2+)肽加合物通过各种生物物理方法进行了研究。（1）H NMR 滴定突出显示了{Ru(CO)(3)}(2+)与 Abeta(28)组氨酸残基的选择性相互作用；圆二色性揭示了 Abeta(28)发生了实质性的构象重排；电喷雾电离质谱（ESI-MS）表明存在普遍的 1:1 金属/肽化学计量比，并揭示了肽结合金属片段的性质。值得注意的是，当 I 与 Abeta(42)反应时，得到了非常相似的 ESI-MS 结果。讨论了上述发现对在阿尔茨海默病中使用钌化合物的可能意义。
