Novel sulfonamide derivatives as multitarget antidiabetic agents: design, synthesis, and biological evaluation
Mohammed Salah Ayoup, Nourhan Khaled, Hamida Abdel‐Hamid, Doaa A. Ghareeb, Samah A. Nasr, Ahmed M. Omer, Amr Sonousi, Asmaa E. Kassab, Abdelazeem S. Eltaweil
Abstract
values of 1.29, 21.38 and 19.03 μM, respectively) exhibited significant glucose uptake activity that were 1.62- to 27-fold more potent than berberine. Both α-glucosidase protein (PDB: 2QMJ) and α-amylase (PDB: 1XCW) complexed with acarbose were adopted for docking investigations for the most active synthesized compounds. The docked compounds were able to inhabit the same space as the acarviosin ring of acarbose. The docking of the most active compounds showed an analogous binding with the active site of α-glucosidase as acarbose. The superior activity of the synthesized compounds against α-glucosidase enzyme than α-amylase enzyme can be rationalized by the weak interaction with the α-amylase. The physiochemical parameters of all synthesized compounds were aligned with Lipinski's rule of five.