摘要
采用荧光光谱法和分子对接法,研究了两种齐墩果酸衍生物与查耳酮的缀合物对α-葡萄糖苷酶的抑制作用及机理.首先,采用荧光光谱法研究了缀合物和α-葡萄糖苷酶的结合反应,并测定了结合常数及相关的热力学参数;然后使用sybyl 8.0软件研究了缀合物与α-葡萄糖苷酶的分子对接.结果表明:缀合物和α-葡萄糖苷酶的相互作用导致α-葡萄糖苷酶发生内源荧光淬灭,属于静态淬灭机制.缀合物1与α-葡萄糖苷酶在20℃和37℃下结合常数分别为42.91和75.42,结合位点均为0.53;缀合物2与α-葡萄糖苷酶在20℃和37℃下结合常数分别为59.88和92.87,结合位点分别为0.5和0.63.缀合物与α-葡萄糖苷酶的结合中氢键和范德华力起重要作用,缀合物能与α-葡萄糖苷酶活性位点结合,作用力主要依靠缀合物酯羰基上的氧原子与酶结构中氨基酸上的氢所形成氢键.
Using fluorescence spectroscopy and molecular docking method, the interaction between two conjugates of oleanolic acid derivatives-chalcones and α-glucosidase were investigated. The binding reaction was studied by fluorescence quenching method, the binding constants, binding site and thermodynamic parameters were calculated, and the molecular docking was performed by the sybyl 8.0. The results showed that endogenous fluorescence quenching of α-glucosidase, which belonged to a static quenching mechanism. The calculated binding constants of conjugate I were 42.91 and 75.42 at 20℃ and 37℃ respectively, and the binding sites were both 0.53. The binding constants of conjugate 2 were 59.88 and 92.87, and the binding sites were 0.5 and 0.63 at 20℃ and 37℃, respectively. The conjugates tended to bind with α-glucosidase mainly by hydrogenbond and van der Waals. Computer molecular docking technology showed that the conjugates binding with the active site of α-glucosidase mainly by hydrogen bonding between oxygen of ester base and hydrogen of amino acid.
出处
《华中师范大学学报(自然科学版)》
CAS
北大核心
2013年第2期204-208,217,共6页
Journal of Central China Normal University:Natural Sciences
基金
中央高校基本科研业务费专项资金项目(CZY12016)