Spectroscopy Study on the Interaction of Colchicine and Human Serum Albumin
MA Jun-yan1,CHEN Ke-hai1,ZHENG Xue-fang1,2*,GUO Ming2,MA Jing1,TANG Qian1,WANG Yu-lian1, HU Jie-han2,3
1. College of Bioengineering, Dalian University, Dalian 116622, China 2. Liaoning Key Lab of Bio-organic Chemistry, Dalian University, Dalian 116622, China 3. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China
Abstract：The binding reaction of colchicine with human serum albumin(HSA) was studied by UV-Vis absorption, fluorescence and circular dichroism spectrometry. The results indicated that colchicine led to the increase in UV absorption and the quenching of intrinsic fluorescence of HSA. As the temperature increased, the quenching constant KSV decreased. The binding constants and the numbers of the binding sites of the interaction between colchicine and HSA at different temperatures were obtained. The thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS), were calculated to be -11.66 kJ·mol-１ and 51.507 J(mol·K)-１ respectively according to Van’t Hoff equation, which suggested that the main binding force between colchicine and HSA was static interaction. The protein conformation was altered(CD date) with decreasing of α-helices in the presence of colchicine. The results showed that the quenching mechanism of the combination of colchicine with human serum albumin was a static quenching procedure.
马君燕1,陈克海1,郑学仿1,2*,郭明2,马静1,唐乾1,王玉莲1,胡皆汉2,3 . 秋水仙碱与人血清白蛋白相互作用的谱学研究[J]. 光谱学与光谱分析, 2007, 27(12): 2485-2489.
MA Jun-yan1,CHEN Ke-hai1,ZHENG Xue-fang1,2*,GUO Ming2,MA Jing1,TANG Qian1,WANG Yu-lian1, HU Jie-han2,3. Spectroscopy Study on the Interaction of Colchicine and Human Serum Albumin. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(12): 2485-2489.
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