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Alzheimer's disease (AD) is the most common form of dementia, a general term for memory loss and other cognitive abilities. This disorder is well associated with an impairment in cholinergic transmission. Therefore, cholinesterase inhibition leads to revert of putative deficit in acetylcholine levels in AD and thus might reverse the memory impairment characteristics. A series of compounds were rationally designed by taking donepezil as a lead molecule by using molecular modeling studies. All the designed compounds were analyzed by calculating their dock scores to check their probable binding affinities within the active site of acetylcholinesterase enzyme. Among all the compounds, six compounds showed significant dock score within the active site of enzyme which suggest that these molecules could effectively block the catalytic activity of enzyme. Compounds with nitro groups on the terminal benzyl moiety were found to be most prominent ones and could act as hit lead for the further development of acetylcholinesterase inhibitors. In silico study of all the compounds were also performed by using computational Marvin Sketch software which describes the compliance of all the designed compounds with the Lipinski rule of five. Furthermore, potent compounds were synthesized and characterized by using 1H & 13C NMR and MASS spectroscopic techniques were sent for further biological evaluations.

A series of twenty-two compounds of thiazole-5-carboxylic acid derivatives was rationally designed and synthesized. All the compounds were characterized by using 1H & 13C NMR and tested against xanthine oxidase enzyme by spectrophotometric assay. Majority of the compounds were found active against the enzyme amongst which GK-20 with an IC50 value of 0.45 μM was found to be most potent. Structure-activity relationship obtained from the biological results revealed that the di-substituted compounds as Ring B were more potent than that of mono- substituted derivatives. Para-substitution on Ring B is crucial for the xanthine oxidase inhibitory potential. Enzyme kinetic studies further revealed their mixed type inhibition behaviour. Moreover, the binding pattern of the most potent compound GK-20 within the febuxostat binding site of the enzyme was further analyzed by using docking studies which revealed that it sufficiently block the catalytic active site which prevents the substrate to bind.