Molecular Docking Study of Chlorogenic Acid as a Hyaluronidase Inhibitor

Hyaluronidases are enzymes degrading hyaluronic acid, which is an important component in all tissues and body fluids. Flexible docking simulation between hyaluronidase and chlorogenic acid as a potent hyaluronidase inhibitor with IC
₅₀
value 2.25mmol/L was performed using ArgusLab docking method and the binding free energy of the docked complex is -10.33 kcal/mol. The binding mode of interaction at the active site was investigated. The hydrogen bonds could be formed between chlorogenic acid and hyaluronidase amino acid residues Glu477 and Glu582. Moreover, there are hydrophobic space interactions between phenyl group of chlorogenic acid and the amino acid residues Ala407 and Val411. This study could be useful for the virtual screening in the development of new hyaluronidase inhibitors.