Molecular docking analysis of Cinnamomum zeylanicum phytochemicals against Secreted Aspartyl Proteinase 4–6 of Candida albicans as anti-candidiasis oral

Abstract

Candida albicans is a polymorphic human microflora species, which caused a candidiasis. This disease frequently occurred in immunocompromised patients with considerable medical outcomes due to the damage from its infections. Secreted Aspartic Proteinase (SAP) 4–6 regulated the virulence of C. albicans. Thus, inhibiting those protenases may useful to obtain a better prognosis. On the other hand, Cinnamomum zeylanicum reported to have anti-cadidiasis. However, the mechanism of action on the anti-cadidiasis activity remains unclear. This study will explain the possible mechanism of anti-candidiasis from the bioactives of C. zeylanicum through SAP 4–6 inhibion. A computational analysis was employed by molecular docking coupled with molecular dynamics simulation to comprehend the interaction among C. zeylanicum bioactives to SAP 4–6. Positive docking outcomes were observed, with Cinnamaldehyde, Pyrantel Hydrochloride, and Hexadecenoic Acidbecame showed promising binding affinity against SAP 4–6. However, those compounds interacted with different residues of each proteinase. Only Hexadenoic Acid bound to the catalytic residues of SAP5-6. Molecular dynamics simulated the stable binding of Hexadecenoid Acid to the SAP5-6. Not only has stable structural integrity, the binding of Hexadecenoic Acidalso showed minimum alterations on the structural stability of SAP5-6, which suggested a stable inhibitory activity. The stable binding of Hexadecenoid Acid also displayed by the prominent number of hydrogen bond and the free-binding energy simulations. In conclusion, the anti-candidiasis activity of C. zeylanicum may take place in the SAP5-6 inhibition, mainly by Hexadecenoic Acid.