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

Maneesh Kumar; Ganesh Chandra Sahoo; Waquar Akhter Ansari; Ajmal Ali Mohammad; Abul Farah Mohammad; Joongku Lee

doi:10.6026/97320630019990

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

Bioinformation. 2023 Oct 31;19(10):990-994. doi: 10.6026/97320630019990. eCollection 2023.

Authors

Maneesh Kumar¹, Ganesh Chandra Sahoo², Waquar Akhter Ansari³, Ajmal Ali Mohammad⁴, Abul Farah Mohammad⁵, Joongku Lee⁶

Affiliations

¹ Department of Biotechnology Magadh University, Bodh Gaya- 824231, Bihar, India.
² ICMR-Rajendra Memorial Research Institute of Medical Sciences, Agamkuan, Patna-800007, Bihar, India.
³ ICAR-Indian Institute of Vegetable Research, Varanasi-221005, Uttar Pradesh, India.
⁴ Department of Botany and Microbiology, College of Science, King Saud University, Riyadh 11451, Saudi Arabia.
⁵ Department of Zoology, College of Science, King Saud University, Riyadh 11451, Saudi Arabia.
⁶ Department of environment and forest resources, Chungnam, National University, Daehak-ro, Yuseong-gu, Daejeon, Republic of Korea.

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.

Keywords: Aflatoxin; O-methyl-transferase; docking; product template.