College of Chemistry and Pharmacy, Qingdao Agriculture University, 266109 Qingdao, People's Republic of China.
Amino Acids. 2010 Mar;38(3):711-9. doi: 10.1007/s00726-009-0275-2. Epub 2009 Apr 4.
The electrochemical behaviors of the interaction of chromotrope 2R (CH2R) with human serum albumin (HSA) are investigated on the hanging mercury drop electrode with linear sweep voltammetry. In the acidic buffer solution (pH 2.5) CH2R has a well-defined voltammetric reductive wave at -0.34 V (SCE). On the addition of HSA into the CH2R solution, the reductive peak current of CH2R decreases with little movement of the peak potential. The voltammetric study shows that the electrochemical parameters of interaction solution do not change and a new electrochemically non-active complex is formed via interaction of CH2R with HSA, which cannot be reduced on the Hg electrode and results in the decrease of the free concentration of CH2R. The decrease of reductive peak current is proportional to HSA concentration and further used for protein detection. The binding ratio and the binding constant are further calculated with the experimental voltammetric data.
采用线性扫描伏安法在悬汞电极上研究了变色酸 2R（CH2R）与人血清白蛋白（HSA）相互作用的电化学行为。在酸性缓冲溶液（pH 2.5）中，CH2R 在-0.34 V（SCE）处有一个明确的还原波。在向 CH2R 溶液中加入 HSA 后，CH2R 的还原峰电流减小，峰电位几乎没有移动。伏安研究表明，相互作用溶液的电化学参数没有改变，并且通过 CH2R 与 HSA 的相互作用形成了新的电化学非活性配合物，该配合物不能在 Hg 电极上还原，导致 CH2R 的游离浓度降低。还原峰电流的减小与 HSA 的浓度成正比，可进一步用于蛋白质检测。进一步根据实验伏安数据计算了结合比和结合常数。
