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• W3148387535 abstract "Aspergillus fungi are known to produce aflatoxins, among which aflatoxin B 1 (AFB 1 ) is the most potent carcinogen that is metabolised by cytochrome P450 (CYP450). In the liver, AFB 1 is metabolised into exo-8,9-epoxide by the CYP1A2 enzymes. The resulting epoxide can react with guanine to cause DNA damage. Natural inhibitors are being identified. However, the modes of action are poorly understood. In the current study, we have investigated the mode of action of AFB 1 with CYP1A2, CYP3A4 and CYP2A13 using molecular dynamic simulation (MD simulation) approaches. The interaction network and paths among CYP1A2, CYP3A4, and CYP2A13 have been investigated using the STRING database and PathLinker plugin of Cytoscape. CYP3A4 is the most active protein involved in interactions with AFB 1 during its metabolism. Residues 362ARG, 445SER, 450LEU and 451PHE of CYP1A2 are important, interacting with AFB 1 and converting it to toxic exo-AFB 1 -8,9-epoxide (AFBEX). The pathway shows that microsomal epoxide hydrolase (EPHX1) may acts as initiator in the signalling pathway where CYP1A2, CYP3A4 and CYP2A13 interact in a sequential order. The interaction network shows there to be a strong association in expression among CYP1A2, CYP3A4 and CYP2A13 along with other metabolising enzymes. The complex of AFB 1 and CYP1A2 was found to be stable during the MD simulation. This study provides a better understanding of the mode of action between AFB 1 and CYP1A2, CYP3A4 and CYP2A13 which relates to the effective management of AFB 1 toxicity. EPHX1 in the protein network may be an ideal target when designing inhibitors to prevent the toxin’s activation. Peptide inhibitors may be designed to block the substrate site residues of CYP1A2 in order to prevent the conversion from AFB 1 into AFBEX. This would either neutralise or reduce its toxicity." @default.
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• W3148387535 date "2021-04-12" @default.
• W3148387535 modified "2023-10-18" @default.
• W3148387535 title "CYP1A2, 2A13, and 3A4 network and interaction with aflatoxin B1" @default.
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• W3148387535 doi "https://doi.org/10.3920/wmj2020.2621" @default.
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