Synthesis, in vitro α-glucosidase and α-amylase activities and molecular docking study of oxadiazole-sulphonamide hybrid analogues

• Published in: Chemical Data Collections Vol. 45; p. 101031
• Main Authors: Ullah, Hayat, Aslam, Muhammad Waseem, Rahim, Fazal, Hussain, Amjad, Perviaz, Muhammad
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.06.2023
• Subjects: molecular docking; Oxadiazoles; structure activity relationship; α-amylase; α-glucosidase; Oxadiazoles; α-glucosidase; α-amylase; molecular docking; structure activity relationship
• ISSN: 2405-8300; 2405-8300
• DOI: 10.1016/j.cdc.2023.101031

Acarbose and voglibose are two different α-glucosidase and α-amylase inhibitors that are used to manage diabetes mellitus. Sadly, these renowned and therapeutically effective inhibitors also have a wide range of negative side effects. Hence, a safer therapy still has to be developed. The current study examines the biological screening of oxadiazole-sulphonamide hybrid analogues (1–14) for their inhibitory action against α-glucosidase and α-amylase enzymes. All analogues showed excellent activities, with IC50 values ranging between 4.30 ± 0.20 to 49.40 ± 0.30 µM (α-glucosidase) and 2.40 ± 0.30 to 21.10 ± 0.50 µM (α-amylase) as compared to the standard drug acarbose (IC50 = 38.45 ± 0.80 and 11.12 ± 0.15 µM, respectively). The most effective α-glucosidase and α-amylase inhibitor was analogue 1 (IC50 = 4.30 ± 0.20 and 2.40 ± 0.30 M, respectively). Molecular docking investigations were carried out to determine the binding mode of the most potent inhibitors with the active site of enzymes.