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目的:采用红外光谱研究曲克芦丁对牛血清白蛋白溶液二级结构的影响。方法:利用红外差谱([蛋白质+药物溶液]-[药物溶液])来研究反应前后蛋白质酰胺带的变化。结果:蛋白质与药物作用后蛋白质分子发生了由螺旋结构向折叠结构的转变。结合蛋白质酰胺Ⅰ带的拟合结果对酰胺Ⅲ带各二级结构的谱峰进行了初步指认:1330~1290 cm-1为α-螺旋;1290~1270 cm-1为β-转角;1270~1250 cm-1为无规则卷曲;1250~1220 cm-1为β-折叠。结论:运用红外光谱的方法研究曲克芦丁和蛋白质的相互作用,为研究其他蛋白质与中药有效成分的相互作用提供一种新的实验方法。
OBJECTIVE: To study the effect of troxerutin on the secondary structure of bovine serum albumin by infrared spectroscopy. Methods: The infrared spectrum ([protein + drug solution] - [drug solution]) was used to study the changes of the amide amide bands before and after the reaction. Results: After the action of protein and drug, the transformation of the protein from helical structure to folded structure took place. The results showed that the peak of the secondary structure of amide Ⅲ with 1330 ~ 1290 cm-1 was α-helix, 1290 ~ 1270 cm-1 was β-turn, and 1270 ~ 1250 cm-1 random curl; 1250 ~ 1220 cm-1 for β-sheet. Conclusion: The interaction between troxerutin and protein was studied by infrared spectroscopy, which provided a new experimental method for studying the interaction between other proteins and the active ingredients of traditional Chinese medicine.