Publications by authors named "Pratik Dhavan"

The synthesis of four new azo-Schiff base ligands from 2-hydroxy-3-methoxy-5-(phenyldiazenyl)benzaldehyde and 4-aminoantipyrine is described in this study. The molecular structures of all the scaffolds were confirmed using NMR spectroscopies such as H and C, as well as FT-IR and Mass spectroscopy. After successful synthesis and characterization of all the ligands, their in vitro antibacterial, antioxidant and anti-inflammatory activities were carried out by using standard protocols.

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Herein, a series of novel antipyrine based α-aminophosphonates derivatives were synthesized and characterized. The synthesized derivatives were subjected for cholinesterase inhibition, enzyme kinetic studies, protein denaturation assay, proteinase inhibitory assay and cell viability assay. For cholinesterase inhibition, the results inferred that the test compounds possess better AChE activity (0.

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A series of novel 2,3,4,5-tetrahydrobenzothiazepine appended α-aminophosphonate derivatives were synthesized by subjecting 2,3-dihydrobenzothiazepine to Pudovik reaction using diethyl phosphite. Tested derivatives exhibited better AChE inhibition (0.86-12.

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A series of novel dihydropyranoindole derivatives containing sulphonamide group were designed, synthesized and evaluated for in-vitro anti-cholinesterase activity. The result showed that all the compounds exhibited potent acetylcholinesterase (AChE) activity (IC = 0.41-8.

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A series of novel carbazole based α-aminophosphonate derivatives were synthesized under solvent-free condition, characterized and evaluated for their cholinesterase inhibition, enzyme kinetic inhibition, cell viability using N2a cells, neuroprotective studies against HO-induced stress using N2a cells and antioxidant studies using DPPH radical activity. Test compounds displayed better AChE activity (0.475 to 7.

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A series of novel N-substituted α-aminophosphonates-bearing chromone moiety were synthesized and evaluated for acetylcholinesterase (AChE), butyrylcholinesterase (BuChE) activities and antioxidant properties. Porcine pancreatic lipase was employed as a catalyst. Inhibitory activity against AChE ranged between 0.

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A series of novel scaffold of N-substituted pyrazole derived α-aminophosphonates were designed, synthesized and evaluated for their anti-cholinesterase activity. Porcine pancreatic lipase (PPL) was used as a catalyst for the organic transformation. Compounds 4ah and 4bh proved to be more potent than the standard drug tacrine, rivastigmine and galantamine for AChE inhibition activity with IC value between 0.

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