Molecular docking analysis of Allium chinense compounds as Secreted Aspartyl Proteinase-5 (SAP5) inhibitor

Abstract

Secreted Aspartyl Proteinase-5 (SAP5) or candidapepsin-5 is known as the current and major virulence factor in the biofilm formation of Candida albicans. The protein is secreted into the environment to disrupt the host immune cells and degrade keratin then penetrating the host defense to express its pathogenicity. SAPs has been targeted for many studies including in vitro test and in silico analysis of potential inhibitory agents. In the current study, we tested six selected compounds in the aqueous extract of Allium chinense G. Don. namely 1-tetradecanol, anozol, hyacinthin, isosorbide, mannitan and oleic acid for in silico analysis along with pepstatin A as the most potent inhibitor or control. The results obtained that oleic acid displayed the most stable bonding with the SAP5 based on molecular docking, visualization and data analysis although slightly lower than anozol in terms of binding affinity. Oleic acid also produced the most similar number of binding residues with pepstatin A based on 2D feature with also similar region in the pocket of SAP5 based on 3D visualization. Hence, the compound may be potentially developed as leading compound in treating C. albicans infections.