New Hybrid Hydrazinyl Thiazole Substituted Chromones: As Potential α-Amylase Inhibitors and Radical (DPPH & ABTS) Scavengers

Abstract

Current research is based on the identification of novel inhibitors of α-amylase enzyme. For that purpose, new hybrid molecules of hydrazinyl thiazole substituted chromones 5–27 were synthesized by multi-step reaction and fully characterized by various spectroscopic techniques such as EI-MS, HREI-MS, 1H-NMR and 13C-NMR. Stereochemistry of the iminic bond was confirmed by NOESY analysis of a representative molecule. All compounds 5–27 along with their intervening intermediates 1–4, were screened for in vitro α-amylase inhibitory, DPPH and ABTS radical scavenging activities. All compounds showed good inhibition potential in the range of IC50 = 2.186–3.405 µM as compared to standard acarbose having IC50 value of 1.9 ± 0.07 µM. It is worth mentioning that compounds were also demonstrated good DPPH (IC50 = 0.09–2.233 µM) and ABTS (IC50 = 0.584–3.738 µM) radical scavenging activities as compared to standard ascorbic acid having IC50 = 0.33 ± 0.18 µM for DPPH and IC50 = 0.53 ± 0.3 µM for ABTS radical scavenging activities. In addition to that cytotoxicity of the compounds were checked on NIH-3T3 mouse fibroblast cell line and found to be non-toxic. In silico studies were performed to rationalize the binding mode of compounds (ligands) with the active site of α-amylase enzyme.

Structural elucidation, molecular docking, α-amylase and α-glucosidase inhibition studies of 5-amino-nicotinic acid derivatives

“…For the most safe and versatile therapeutic solutions, we diverged into the plethora of naturally occurring medicinal compounds, specifically, nitrogen containing heterocyclic rings. Piperidine, pyridine and pyrimidine derivatives have been known to inhibit carbohydrate digesting enzymes, in addition to their anti-inflammatory, antibacterial and anticancer potencies [13][14][15][16][17][18][19][20].…”

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“…The reaction was arrested by heating samples at 90 to 100 °C. The quantity of glucose was determined by the GOD-POD method at 546 nm 23 . Enzyme activity hinges upon the amount of glucose released.…”

In vitro and in silico studies of bis (indol-3-yl) methane derivatives as potential α-glucosidase and α-amylase inhibitors

“… 6–7 α-Amylase (E.C.3.2.1.1), one hydrolase enzyme, is mainly secreted by the pancreas and salivary glands. 8–9 α-Amylase catalytic hydrolyse the starch to produces maltose and glucose by breaking α-1,4-glucosidic bonds. 10–11 The inhibition the activity of α-glucosidase or α-amylase delay the hydrolase of polysaccharides, consequently, the postprandial blood glucose level can be reduced, which is believed as an effective approach for the treatment strategy of DM.…”