The inhibitory mechanism of engeletin against α-glucosidase was investigated for the first time by fluorescence spectroscopy and molecular docking. The results showed that engeletin could inhibit α-glucosidase in a noncompetitive inhibition mode with a half-maximal inhibitory concentration value of 48.5 ± 6.0 µg/mL (0.11 ± 0.014 mmol/L). It was found that engeletin could cause static fluorescence quenching of α-glucosidase by forming a complex with α-glucosidase. The thermodynamic parameters indicated that the combination of engeletin and α-glucosidase was driven by hydrophobic force. The molecular docking results confirmed that some amino acid residues of α-glucosidase (Trp391, Arg428, Glu429, Gly566, Trp710, Glu771) could interact with engeletin by hydrogen bonding.

通过荧光光谱和分子对接首次研究了恩格列汀对α-葡萄糖苷酶的抑制机理。结果表明，恩格列汀可以以非竞争性抑制方式抑制α-葡萄糖苷酶，其最大抑制浓度值的一半为48.5±6.0 µg / mL（0.11±0.014 mmol / L）。发现恩格列汀可通过与α-葡萄糖苷酶形成复合物而引起α-葡萄糖苷酶的静态荧光猝灭。热力学参数表明恩格列汀和α-葡萄糖苷酶的结合是由疏水力驱动的。分子对接结果证实，α-葡糖苷酶的某些氨基酸残基（Trp391，Arg428，Glu429，Gly566，Trp710，Glu771）可以通过氢键与恩格列汀相互作用。