Streptomyces tetracycline’s computational behavior against polyketide synthase of aflatoxigenic fungi

Abstract

produces a variety of bioactive compounds that prevent fungal growth, including aflatoxins. Aflatoxigenic fungi ( and ) are being researched concerning spp. and can prevent the spread of aflatoxins-producing fungi. Aflatoxin-degrading enzymes, which can convert poisonous aflatoxins into less dangerous compounds, are also produced by spp. The processes through which these microorganisms can be used to reduce aflatoxins in food and agricultural systems are still the subject of active research. To evaluate the novelty of tetracycline against the biosynthesis of aflatoxin in aflatoxigenic fungi via computational approach. In this study, we performed molecular docking of polyketide synthase (Pks-A), an enzyme that initiates aflatoxin biosynthesis using tetracycline, using the online SeamDock server. Our results showed that tetracycline had a strong affinity for Pks-A in the binding pocket. The binding energy of tetracycline was -12.7 kcal/mol, indicating a strong binding affinity between the two molecules. Furthermore, the binding site was located in the active site, which is a conserved region in Pks-A and is essential for catalysing the formation of aflatoxin. The results of our docking study suggest that tetracycline may be an effective inhibitor of aflatoxin biosynthesis.