Department of Chemistry, Susquehanna University, Selinsgrove, PA 17870, USA.
Dalton Trans. 2012 Mar 7;41(9):2720-31. doi: 10.1039/c2dt12169g. Epub 2012 Jan 16.
A series of twelve anionic, cationic, and neutral nickel(II) complexes have been synthesized and characterized. The interaction of these complexes with bovine serum albumin (BSA), human serum albumin (HSA), lysozyme (Lyso), and tryptophan (Trp) has been studied using steady-state fluorescence spectroscopy. Dynamic and static quenching constants have been calculated, and the role played in quenching by the ligand and complex charge investigated. The nickel complexes showed selectivity towards the different proteins based on the environment surrounding the Trp residue(s). Only small neutral complexes with hydrophobic ligands effectively quenched protein fluorescence via static quenching, with association constants ranging from 10(2) M(-1) (free Trp) to 10(10) M(-1) (lysozyme), indicating a spontaneous and thermodynamically favorable interaction. The number of binding sites, on average, was determined to be one in BSA, HSA and free Trp, and two in lysozyme.
已经合成并表征了一系列十二种阴离子、阳离子和中性镍（II）配合物。使用稳态荧光光谱法研究了这些配合物与牛血清白蛋白（BSA）、人血清白蛋白（HSA）、溶菌酶（Lyso）和色氨酸（Trp）的相互作用。计算了动态和静态猝灭常数，并研究了配体和配合物电荷在猝灭中所起的作用。镍配合物根据色氨酸残基周围的环境表现出对不同蛋白质的选择性。只有小的中性配合物具有疏水性配体，通过静态猝灭有效地猝灭蛋白质荧光，其结合常数范围从 10(2) M(-1)（游离色氨酸）到 10(10) M(-1)（溶菌酶），表明这是一种自发的和热力学有利的相互作用。在 BSA、HSA 和游离色氨酸中，平均结合位点数为一个，在溶菌酶中为两个。
