A series of symmetrical salicylaldehyde-bishydrazine azo molecules,
5a–
5h, have been synthesized, characterized by
1H-NMR and
13C-NMR, and evaluated for their in vitro α-glucosidase and α-amylase inhibitory activities. All the synthesized compounds efficiently inhibited both enzymes. Compound
5g was
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A series of symmetrical salicylaldehyde-bishydrazine azo molecules,
5a–
5h, have been synthesized, characterized by
1H-NMR and
13C-NMR, and evaluated for their in vitro α-glucosidase and α-amylase inhibitory activities. All the synthesized compounds efficiently inhibited both enzymes. Compound
5g was the most potent derivative in the series, and powerfully inhibited both α-glucosidase and α-amylase. The IC
50 of
5g against α-glucosidase was 0.35917 ± 0.0189 µM (standard acarbose IC
50 = 6.109 ± 0.329 µM), and the IC
50 value of
5g against α-amylase was 0.4379 ± 0.0423 µM (standard acarbose IC
50 = 33.178 ± 2.392 µM). The Lineweaver-Burk plot indicated that compound
5g is a competitive inhibitor of α-glucosidase. The binding interactions of the most active analogues were confirmed through molecular docking studies. Docking studies showed that
5g interacts with the residues Trp690, Asp548, Arg425, and Glu426, which form hydrogen bonds to
5g with distances of 2.05, 2.20, 2.10 and 2.18 Å, respectively. All compounds showed high mutagenic and tumorigenic behaviors, and only
5e showed irritant properties. In addition, all the derivatives showed good antioxidant activities. The pharmacokinetic evaluation also revealed promising results
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