Molecular Docking and ADMET Analysis of Bioactive Compounds from Aspergillus nomius NC06 Against Plasmepsin Protein: Antimalarial Activity

Abstract

The development of new antimalarial drugs is urgently needed. The marine sponge-derived fungus Aspergillus nomius NC06 is known to have bioactive compounds including aspergillicin A, oxisterigmatocystine J, oxisterigmatocystine K and oxisterigmatocystine L. In this study, we performed a virtual screening of bioactive compounds from A. nomius NC06 by molecular docking and adsorption, distribution, metabolism, excretion and toxicity analysis against plasmepsin I, IV and V proteins to observe their antimalarial activity. Plasmepsin protein is considered an important drug target due to its essential role in protein export. The results showed that aspergillicin A had the potential to inhibit Plms I, IV and V proteins, with the highest negative binding affinity values at -10.0, -10.3 and -10.7 kcal moL-1, respectively. The binding affinity was supported by the formation of hydrogen bonds and hydrophobic interactions. In addition, artemisinin as a positive control has a binding affinity of about -7.4 kcal moL-1, suggesting that the compounds isolated from the marine sponge have the potential to combat malaria and could be developed as lead compounds for anti-malarial therapy.