【摘要】 目的:探讨棉酚与人血清白蛋白(HSA)的相互作用。方法:采用荧光光谱方法研究在生理条件下,棉酚与人血清白蛋白(HSA)的相互作用,并采用分子对接软件模拟棉酚与人血清白蛋相互作用。结果:棉酚与HSA的结合常数为2.390 6×105L·mol-1(293K)和3.576 8×103L·mol-1(303K),具有一个结合位点,结合反应的主要作用力为氢键和范德华力,结合位置更接近于人血清白蛋白的酪氨酸残基,分子模拟分析也证实此结果。结论:棉酚对人血清白蛋白的荧光猝灭机制属于静态荧光猝灭。更多还原

【Abstract】 Objective: To explore the interaction between gossypol and human serum albumin( HSA). Methods: The interaction of gossypol and HSA under physiological conditions was studied by fluorescence spectroscopy,and the molecular docking software was used to simulate the interaction. Results: The binding constant of gossypol and HSA at 293 K and 303 K was 2. 390 6 × 105L·mol- 1and 3. 576 8 × 103L·mol- 1,respectively. There was one binding site on HSA for gossypol. Hydrogen bond and Van Der Waals interactions were involved in the binding process. The binding of gossypol and HAS was closer to tyrosine residue in HSA. The molecular simulation analysis verified the above results. Conclusion: The gossypol-induced fluorescence quenching of HSA belongs to a static quenching procedure.更多还原