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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。
Objective: To investigate the interaction between gossypol and human serum albumin (HSA). Methods: The interaction between gossypol and human serum albumin (HSA) under physiological conditions was studied by fluorescence spectroscopy. The interaction between gossypol and human serum albumin was simulated by molecular docking software. Results: The binding constants of gossypol and HSA were 2.390 6 × 105L · mol-1 (293K) and 3.576 8 × 103L · mol-1 (303K), respectively, with a binding site. The main binding forces were hydrogen bonding and Van der Waals force, binding sites closer to the human serum albumin tyrosine residues, molecular modeling analysis also confirmed this result. Conclusion: The fluorescence quenching mechanism of gossypol to human serum albumin belongs to static fluorescence quenching.