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The targeted compounds in this research, resveratrol analogs 1 - 14 , were synthesized as mixtures of isomers by the Wittig reaction using heterocyclic triphenylphosphonium salts and various benzaldehydes. The planned compounds were those possessing the trans -configuration as the biologically active trans -resveratrol. The pure isomers were obtained by repeated column chromatography in various isolated yields depending on the heteroaromatic ring. It was found that butyrylcholinesterase (BChE) was more sensitive to the heteroaromatic resveratrol analogs than acetylcholinesterase (AChE), except for 6 , the methylated thiophene derivative with chlorine, which showed equal inhibition toward both enzymes. Compounds 5 and 8 achieved the highest BChE inhibition with IC 50 values of 22.9 and 24.8 μM, respectively. The same as with AChE and BChE, methylated thiophene subunits of resveratrol analogs showed better enzyme inhibition than unmethylated ones. Two antioxidant spectrophotometric methods, DPPH and CUPRAC, were applied to determine the antioxidant potential of new heteroaromatic resveratrol analogs. The molecular docking of these compounds was conducted to visualize the ligand-active site complexes' structure and identify the non-covalent interactions responsible for the complex's stability, which influence the inhibitory potential. As ADME properties are crucial in developing drug product formulations, they have also been addressed in this work. The potential genotoxicity is evaluated by in silico studies for all compounds synthesized.

New 1,2,3-triazolo(thieno)stilbenes were synthesized as mixtures of isomers and efficiently photochemically transformed to their corresponding substituted thienobenzo/naphtho-triazoles in high isolated yields. The resulting photoproducts were studied as acetyl- (AChE) and butyrylcholinesterase (BChE) inhibitors without or with interconnected inhibition potential of TNF-α cytokine production. The most promising anti-inflammatory activity was shown again by naphtho-triazoles, with a derivative featuring 4-pentenyl substituents exhibiting notable potential as a cholinesterase inhibitor. To identify interactions between ligands and the active site of cholinesterases, molecular docking was performed for the best potential inhibitors. Additionally, molecular dynamics simulations were employed to assess and validate the stability and flexibility of the protein-ligand complexes generated through docking.