Synthesis, molecular docking, assessment of biological and anti-diabetic properties of benzalacetophenone derivatives.

The current study compares the environmental impact of benzalacetophenone derivatives synthesized using conventional and nanomaterial-catalyzed techniques. Non-isolable thia-Michel adducts are produced when chalcone 1 reacts with thiourea thiolate anion; thiazine 2 is then obtained by cyclocondensation and dehydrogenation. Depending on the pH of the medium, hydrazine and target 1 can undergo pyrazole heterocyclization followed by N-acylation to produce compounds 3, 4, and 5. N-benzoylpyrazole derivative 6 was produced when compound 1 was allowed to condense with benzoylhydrazide. Hydroxylamine hydrochloride and chalcone 1 undergo cyclo-condensation, which releases H(2)O and yields an isoxazole derivative 7. After cyclizing cyanoacetohydrazide via the α, β-unsaturated system and adding a cyclic imino moiety to the cyano functionality, product 8 is produced. Thioamide derivative 9 was made by the interaction of Target 1 with thiosemicarbazide. Acid caused 1 to cyclize with 2-aminothiophenol, forming thiazapine 10. Michel's addition initiated this process, which was followed by intramolecular cyclocondensation. Diazapines 11 and 12 were produced when compound 1 reacted with o-phenylenediamine and 3-nitro-o-phenylenediamine in a basic media. Reaction times and product yields were enhanced in several studies by using nanoparticles in place of conventional catalysts. Azoles and their derivatives are significant members of the organic chemical class due to their broad biological and pharmacological significance. All of the produced compounds exhibited strong antioxidant activity against DPPH and H(2)O(2) radicals and noticeably higher activity against SOR and NO radicals when compared to regular ascorbic acid. Furthermore, the biological experiments that demonstrated the action of compounds 2, 3, and 10 were corroborated by molecular docking analyses utilizing the MOE software, GacH as a maltose/maltodextrin-binding protein, and acarbose as the reference ligand.