New amino acid clubbed Schiff bases inhibit carbonic anhydrase II, α-glucosidase, and urease enzymes: in silico and in vitro

Combating pathological conditions related to hyperactivity of enzymes remains a formidable challenge for health. Small molecules therapy constitutes one of the means to circumvent the medical disorders resulting from enzyme hyperactivity. In this regard, we have synthesized structurally diverse amino acid hybrid Schiff bases (5a-5l and 10a-10k) and evaluated them for carbonic anhydrase II, alpha-glucosidase, and urease inhibitory potential. These new chemical scaffolds showed variable efficacies against the selected enzymes. The results indicated that compounds 5b (11.8 +/- 1.33 mu M), 10i (83.3 +/- 1.13 mu M), and 10f (88.2 +/- 2.27 mu M) are the most active scaffolds against carbonic anhydrase II, alpha-glucosidase, and urease, respectively. A structure-activity relationship revealed the most structural features contributing to the overall activities. Molecular docking suggested that these compounds possess excellent binding interactions with the active site residues of the targets by interacting through hydrogen bonding, pi-pi, and pi-cation interactions.

Automated summary

The study synthesized structurally diverse amino acid hybrid Schiff bases and evaluated their inhibitory potential against selected enzymes. Results showed certain compounds exhibited high activity against the enzymes. Analysis of structure-activity relationship and molecular docking revealed the inhibitory mechanisms of these compounds.