Nursing

Catalysis

Acarbose

Amylase

Carbon-13 NMR

Active site

Imine

Biochemistry

Molecule

Docking (animal)

Alpha-amylase

Stereochemistry

Organic chemistry

Thiazolidine

In vitro

Enzyme

Semicarbazone

Proton NMR

IC50

Medicine

Chemistry

Hydrogen bond

Journal of Molecular Structure

Benzohydrazide based imine derivatives (1c-16c) and thiazolidine-4-one derivatives (1d-16d) were synthesized and characterized with different spectroscopic techniques i.e. HREI-MS, 1HNMR and 13CNMR. The synthesized analogs were examined for antidiabetic potential and hence evaluated against α-glucosidase and α-amylase enzyme. Benzohydrazide based imine derivatives showed outstanding α-glucosidase inhibition ranging from 5.60 ± 0.30 to 38.10 ± 0.30 µM when compared with acarbose (IC50 = 38.45 ± 0.80 µM). Compound 5c (IC50 = 5.60 ± 0.30 µM) has m/p-dihydroxyl groups at phenyl ring while compound 15c (IC50 = 7.30 ± 0.10 µM) has one p‑hydroxyl group present at phenyl ring were most potent in the imine series. Molecular docking study further support that hydrogen bonding is predominant. Thiazolidin-4-one derivatives (1d-16d) were screen against α-amylase enzyme and were found to show excellent potential with IC50 values ranging from 0.40 ± 0.05 to 22.11 ± 1.20 µM when compared with standard acarbose (IC50 = 0.91 ± 0.20 µM). The most potent analog in the series was 5d (IC50 = 0.40 ± 0.05 µM) when compared with standard. Molecular docking study was carried out for active site determination and to rationalize the activities of the active compounds.

In vitro α-glucosidase and α-amylase inhibitory potential and molecular docking studies of benzohydrazide based imines and thiazolidine-4-one derivatives