Molecular docking analysis of Omt-A protein model from Aspergillus flavus with synthetic compounds.

ABSTRACT: Aflatoxin is a potent mycotoxin of Aspergillus flavus that has been classified as a Group I carcinogen. O-methyltransferase A (Omt-A) is a critical enzyme in the formation of aflatoxin. It catalyzes the methylation of norsalic acid to form the highly toxic intermediate averantin. The ligand-protein interaction of Omt-A was performed with piperlonguminin and blasticidins. The maximum affinity of -10.6 was found for the 5ICC_A piperlonguminine at site1 (X,Y,Z: -15.282, 21.785, 5.672). Compounds such as Blasticidin S, Neoeriocitrin, Blasticidin S - hydrochloric acid, 6,6''-Bigenkwanin, Pipernomaline, and Eriodictyol were found to have binding features to protein residues, as shown by computational interaction at the molecular level.

SUBMITTER: Kumar M 

PROVIDER: S-EPMC10640793 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature