Trynda-Lemiesz L, Karaczyn A, Keppler B K, Kozłowski H
Faculty of Chemistry, University of Wrocław, Poland.
J Inorg Biochem. 2000 Mar;78(4):341-6. doi: 10.1016/s0162-0134(00)00062-3.
The interactions between HInd[RuInd2Cl4] and human serum albumin have been investigated through UV-Vis, circular dichroism (CD), fluorescence spectroscopy and the inductively coupled plasma-atomic emission spectroscopy (ICP(AES)) method. Binding of Ru(III)-indazole species to albumin has strong impact on protein structure and it influences considerably albumin binding of other molecules like warfarin, heme or metal ions. The metal complex-human serum albumin (HAS) interactions cause conformational changes with loss of helical stability of the protein and local perturbation in the domain IIA binding pocket. The relative fluorescence intensity of the ruthenium-bound HSA decreased, suggesting that perturbation around the Trp 214 residue took place. This was confirmed by the destabilization of the warfarin-binding site, which includes Trp 214, observed in the metal-bound HSA.
通过紫外可见光谱、圆二色光谱（CD）、荧光光谱以及电感耦合等离子体原子发射光谱（ICP（AES））方法研究了HInd[RuInd2Cl4]与人血清白蛋白之间的相互作用。Ru（III）-吲唑物种与白蛋白的结合对蛋白质结构有强烈影响，并且显著影响其他分子如华法林、血红素或金属离子与白蛋白的结合。金属配合物与人血清白蛋白（HSA）的相互作用导致蛋白质构象发生变化，螺旋稳定性丧失，并且在结构域IIA结合口袋中产生局部扰动。结合钌的HSA的相对荧光强度降低，表明色氨酸214残基周围发生了扰动。在结合金属的HSA中观察到的包括色氨酸214的华法林结合位点的不稳定证实了这一点。
