Spectroscopic and Docking Studies on the Binding of Liquiritigenin with Hyaluronidase for Antiallergic Mechanism.
The inhibitory effect of liquiritigenin on hyaluronidase and its binding mechanism were investigated systematically by UV-vis absorption, fluorescence, and molecular modeling approaches. These results indicated that liquiritigenin could interact with hyaluronidase to form a liquiritigenin-hyaluronidase complex. The binding constant, number of binding sites, and thermodynamic parameters were calculated, which indicated that liquiritigenin could spontaneously bind with hyaluronidase mainly through electrostatic and hydrophobic interactions with one binding site. Synchronous fluorescence, three-dimensional fluorescence, and molecular docking results revealed that liquiritigenin bound directly to the enzyme cavity site and this binding influenced the microenvironment of the hyaluronidase activity site, resulting in reduced hyaluronidase activity. The present study provides useful information for clinical applications of liquiritigenin as a hyaluronidase inhibitor.
School of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450001, China.
Hua-Jin
HJ
Zeng
College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou 450001, China.
Ran
R
Yang
School of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450001, China.
Jing
J
You
College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou 450001, China.
Ling-Bo
LB
Qu
College of Chemistry and Molecular Engineering, Zhengzhou University, Zhengzhou 450001, China.
Yan-Jun
YJ
Sun