利用紫外-可见光谱、傅里叶变红外光谱、圆二色谱和分子建模技术研究了考马斯亮蓝G-250与牛血清白蛋白（BSA）的相互作用。紫外-可见光谱测定结果表明，随BSA的浓度的增加，以1:1形成复合物，在不同温度条件下，结合形成常数值分别为5.03×104、3.04×104、2.84×104和1.99×104 L/mol，随温度升高而减小，整个反应过程是焓、熵联合驱动自发进行，热力学焓变（ΔH）和熵变（ΔS）分别为-45.3229 kJ/mol和-139.1847 J/(K?mol)，说明分子间作用力以氢键和范德华力为主；采用傅里叶红外技术研究了作用前后BSA中α-螺旋特征酰胺带（I和II）的变化，结果表明酰胺带I由1650 cm-1移动到1710 cm-1，酰胺带II从1544 cm-1移动到1573 cm-1，α-螺旋结构降低；圆二色谱测定结果和分子对接技术进一步验证了BSA结构的变化，α-螺旋含量由42.15%下降至1.27%。

The interaction of Coomassie brilliant blue G-250 (CBBG-250) with bovine serum albumin (BSA) was investigated by the methods of ultraviolet-visible (UV-Vis) spectroscopy, Fourier transform infrared spectroscopy (FT-IR), circular dichroism (CD), and molecular modeling technique. The UV-Vis results showed that BSA could interact with CBBG-250 to form a CBBG-BSA complex in a molar ratio of 1:1 with increasing BSA concentrations. At different temperatures, the apparent binding constant (Ka) values were 5.03 ? 104 (298 K), 3.04 ? 104 (303 K), 2.84 ? 104 (308 K), and 1.99 ? 104 L/mol (313 K), respectively, which decreased with increasing temperatures. The whole process was enthalpically and entropically driven, and the enthalpy (△H) and entropy changes (△S) were 45.32 kJ/mol and 139.18 J/(mol?K), respectively, indicating that the hydrogen bonds and Van der Waals forces played a dominant role in the molecular interaction. FT-IR was used to study the changes in characteristic amide bands (I and II) of α-helix in BSA before and after the interaction. The results showed that amide band I shifted from 1650 cm-1 to 1710 cm-1, amide band II shifted from 1573 cm-1 to 1544 cm-1, and the α-helical structure content was reduced. CD measurements and molecular docking technique further verified the changes in BSA structure and the content of α-helical structure decreased from 42.15% to 1.27%.

农业行业科研专项(201203042)；国家自然基金资助项目(31060041,51366009)；甘肃省自然基金（1212RJYA008，1212RJYA034）；兰州理工大学“红柳青年教师培养计划”(Q201207)