Mushroom tyrosinase enzyme catalysis: synthesis of larvicidal active geranylacetone derivatives against Culex quinquesfasciatus and molecular docking studies

The grindstone process, which uses tyrosinase as a catalyst, was used to create analogues of geranylacetone. Tyrosinase was used to prepare the Mannich base under favourable reaction conditions, resulting in a high yield. All synthesized compounds were characterized using FTIR, Nuclear magnetic resonance, and mass spectral analyses. The active geranylacetone derivatives ( ) were investigated for larvicidal activity against ; compound (LD :20.7 μg/mL) was noticeably more effective than geranylacetone (LD : >100 μg/mL) and permethrin (LD : 24.4 μg/mL) lead compounds because of their ability to kill larvae and use them as pesticides. All compounds were found to be low toxic, whereas compounds , and were screened for antifeedant screening of non -aquatic target for the toxicity measurement against marine fish at 100 μg/mL caused 0% mortality in within 24 h. Molecular docking studies of synthesised compound and permethrin docked with 3OGN, compound demonstrated a greater binding affinity (-9.6 kcal/mol) compared to permethrin (-10.5 kcal/mol). According to these results, the newly synthesised geranylacetone derivatives can serve as lead molecules of larvicides agents.