Yue Yuanyuan, Chen Xingguo, Qin Jin, Yao Xiaojun
Department of Chemistry, Lanzhou University, Lanzhou 730000, PR China.
Colloids Surf B Biointerfaces. 2009 Feb 15;69(1):51-7. doi: 10.1016/j.colsurfb.2008.10.016. Epub 2008 Nov 6.
This study was designed to examine the interaction of oxaliplatin with human serum albumin (HSA) under physiological conditions by using fluorescence, absorption, FT-IR and circular dichroism (CD) spectroscopic techniques in combination with molecular docking study. Spectroscopic analysis of the emission quenching at different temperatures has revealed that the quenching mechanism of oxaliplatin with HSA was static quenching mechanism. The value of 1.64nm for the distance r between the donor (HSA) and acceptor (oxaliplatin) was derived from the fluorescence resonance energy transfer. From the CD and FT-IR results, it was apparent that the interaction of oxaliplatin with HSA caused a conformational change of the protein. Molecular docking study showed that oxaliplatin bind to residues located in subdomain IIA of HSA. The effect of metal ions and amino acids on the binding constant of HSA-oxaliplatin complex was also discussed.
本研究旨在通过荧光、吸收、傅里叶变换红外光谱（FT-IR）和圆二色光谱（CD）技术，并结合分子对接研究，考察在生理条件下奥沙利铂与人血清白蛋白（HSA）的相互作用。对不同温度下发射猝灭的光谱分析表明，奥沙利铂与HSA的猝灭机制为静态猝灭机制。供体（HSA）与受体（奥沙利铂）之间的距离r值为1.64nm，由荧光共振能量转移得出。从CD和FT-IR结果可以明显看出，奥沙利铂与HSA的相互作用导致了蛋白质的构象变化。分子对接研究表明，奥沙利铂与位于HSA亚结构域IIA中的残基结合。还讨论了金属离子和氨基酸对HSA-奥沙利铂复合物结合常数的影响。
