Zhang Yao-Dong, Gao Qun-Qun, Yu Cai-Hong
Key Laboratory of Analytical Chemistry for Life Science of Shaanxi Province, School of Chemistry and Materials Science, Shaanxi Normal University, Xi'an 710062, China.
Yao Xue Xue Bao. 2011 Jun;46(6):677-82.
The interaction between genistein and beta-glucosidase was studied using fluorescence quenching method and synchronous fluorimetry. The binding reaction was simultaneously studied by the AutoDock 4.2 molecular docking model. Data from fluorescence spectroscopy indicated that these interactions resulted in the endogenous fluorescence quenching of beta-glucosidase, which belongs to a static quenching mechanism. The calculated binding constants were 3.69 x 10(4), 3.06 x 10(4) and 2.36 x 10(4) L x mol(-1) at 17, 27 and 37 degrees C, respectively. The evidences from synchronous fluorescence showed the effect of genistein on the microenvironment around beta-glucosidase in aqueous solution. The inhibition test showed that the activity of beta-glucosidase could be inhibited by genistein. The determined bimolecular rate constant (k(i)) was 1.2 x 10(3) (mol x L(-1)(-1) x min(-1). Molecular docking was performed to reveal the possible binding mode or mechanism and suggested that genistein could bind strongly to beta-glucosidase. The results revealed that genistein tended to bind with beta-glucosidase mainly by hydrogen bond and hydrophobic interaction as well as electrostatic forces.
采用荧光猝灭法和同步荧光法研究了染料木黄酮与β-葡萄糖苷酶之间的相互作用。同时利用AutoDock 4.2分子对接模型研究了两者的结合反应。荧光光谱数据表明，这些相互作用导致β-葡萄糖苷酶的内源荧光猝灭，属于静态猝灭机制。在17、27和37℃下计算得到的结合常数分别为3.69×10⁴、3.06×10⁴和2.36×10⁴ L·mol⁻¹。同步荧光的结果表明了染料木黄酮对水溶液中β-葡萄糖苷酶周围微环境的影响。抑制试验表明，染料木黄酮可抑制β-葡萄糖苷酶的活性。测定的双分子速率常数（k(i)）为1.2×10³（mol·L⁻¹⁻¹·min⁻¹）。进行分子对接以揭示可能的结合模式或机制，结果表明染料木黄酮可与β-葡萄糖苷酶强烈结合。结果表明，染料木黄酮倾向于主要通过氢键、疏水相互作用以及静电力与β-葡萄糖苷酶结合。
