等温滴定量热法
化学
位阻效应
人血清白蛋白
对接(动物)
疏水效应
分子结合
立体化学
茶碱
滴定法
分子模型
结合位点
空间因子
分子
计算化学
有机化学
色谱法
物理化学
生物化学
医学
护理部
内分泌学
作者
Xinluan Lv,Wenjin Li,Miao Zhang,Ruiyong Wang,Junbiao Chang
摘要
Abstract The binding of four alkaloids with human serum albumin (HSA) was investigated by isothermal titration calorimetry (ITC), spectroscopy and molecular docking techniques. The findings demonstrated that theophylline or caffeine can bind to HAS, respectively. The number of binding sites and binding constants are obtained. The binding mode is a static quenching process. The effects of steric hindrance, temperature, salt concentration and buffer solution on the binding indicated that theophylline and HSA have higher binding affinity than caffeine. The fluorescence and ITC results showed that the interaction between HSA and theophylline or caffeine is an entropy‐driven spontaneous exothermic process. The hydrophobic force was the primary driving factor. The experimental results were consistent with the molecular docking data. Based on the molecular structures of the four alkaloids, steric hindrance might be a major factor in the binding between HSA and these four alkaloids. This study elucidates the mechanism of interactions between four alkaloids and HSA.
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