MODELING P1-M BINDING TO ENZYMES OF THE CHITIN DEGRADATION PATHWAY IN ASIAN CORN BORER, Ostrinia furnacalis (Guenee)
Discovery and development of new mode of action chemical entities is important for increasing the number of effective tools for management of insect resistance to insecticides. Inverse in silico molecular docking was utilized to identify possible enzyme targets of P1-M in O. furnacalis. Tight binding interaction of P1-M was observed in chitinase ( -8.6 kcal/mol) and β-N-Acetyl-d-hexosaminidase ( -8.1 kcal/mol), respectively. Hydrogen bonding and hydrophobic interactions contributed by the amphiphilic property of P1-M resulted in tight binding in the active site of the target enzymes. Molecular interaction of P1-M with O. furnacalis chitin synthase could not be properly evaluated because of the lack of accurate model of its 3D structure. Taken together, the structure-based in silico docking study revealed that P1-M is a possible strong inhibitor of enzymes responsible for chitin degradation pathway in O. furnacalis.
Key words: in silico, P1-M, inverse virtual docking, mode of action, P1-M
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