New quinoline-based triazole hybrid analogs as effective inhibitors of α-amylase and α-glucosidase: Preparation, evaluation, and molecular docking along with studies.

The 7-quinolinyl-bearing triazole analogs were synthesized and further assessed for their inhibitory profile against α-amylase andα-glucosidase. The entire analogs showed a diverse range of activities having IC values between 0.80 ± 0.05 µM to 40.20 ± 0.70 µM (α-amylase) and 1.20 ± 0.10 µM to 43.30 ± 0.80 µM (α-glucosidase) under the positive control of acarbose (IC = 10.30 ± 0.20 µM) (IC = 9.80 ± 0.20 µM as the standard drug. Among the synthesized scaffolds, seven scaffolds , , , , , , and showed excellent α-amylase and α-glucosidase inhibitory potentials with IC values of 4.30 ± 0.10, 2.10 ± 0.10, 1.80 ± 0.10, 1.50 ± 0.10, 0.80 ± 0.05, 5.30 ± 0.20, and 6.40 ± 0.30 µM (against α-amylase) and 3.30 ± 0.10, 2.40 ± 0.10, 1.20 ± 0.10, 1.90 ± 0.10, 8.80 ± 0.20, 7.30 ± 0.40, and 5.50 ± 0.10 µM (against α-glucosidase), respectively, while the remaining 12 scaffolds , , , , , , , , , , and   showed less α-amylase and α-glucosidase inhibitory potentials than standard acarbose but still found to be active. Structure-activity connection studies also showed that scaffolds with electron-withdrawing groups like -Cl, -NO, and -F linked to the phenyl ring had higher inhibitory potentials for -amylase and -glucosidase than scaffolds with -OCH, -Br, and -CH moieties. In order to better understand their binding sites, the powerful scaffolds and were also subjected to molecular docking studies. The results showed that these powerful analogs provide a number of important interactions with the active sites of both of these targeted enzymes, including conventional hydrogen bonding, pi-pi stacking, pi-sulfur, pi-anion, pi-pi, pi-sigma, T-shaped, and halogen (fluorine). Furthermore, various techniques (spectroscopic), including 1H, C-NMR, and HREI-MS mass, were used to explore the correct structure of newly afforded hybrid scaffolds based on quinoline-bearing triazole ring.