Synthesis, α-amylase and α-glucosidase inhibition and molecular docking studies of indazole derivatives. Issue 21 (5th December 2022)

• Record Type: Journal Article
• Authors: Nawaz, Muhammad; Taha, Muhammad; Qureshi, Faiza; Ullah, Nisar; Selvaraj, Manikandan; Shahzad, Sumaira; Chigurupati, Sridevi; Abubshait, Samar A.; Ahmad, Tauqir; Chinnam, Sampath; Hisaindee, Soleiman
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 40:Issue 21(2022)
• Page Start: 10730
• Page End: 10740
• Publication Date: 2022-12-05
• Subjects: Indazole -- α-amylase activity -- α-glucosidase activity -- molecular docking -- spectral studies -- NMR -- HR-MS -- FTIR; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2021.1947892
• Languages: English
• ISSNs: 0739-1102

Abstract

Abstract: Herein, we report the synthesis and inhibitory potential of indazole (Methyl 1 H -indazole-4-carboxylate) derivatives (1–13 ) against α-amylase and α-glucosidase enzymes. The described derivatives demonstrated good inhibitory potential with IC50 values, ranging between 15.04 ± 0.05 to 76.70 ± 0.06 µM ± SEM for α-amylase and 16.99 ± 0.19 to 77.97 ± 0.19 µM ± SEM for α-glucosidase, respectively. In particular, compounds (8 –10 and 12 ) displayed significant inhibitory activities against both the screened enzymes, with their inhibitory potential comparable to the standard acarbose (12.98 ± 0.03 and 12.79 ± 0.17 µM ± SEM, respectively). Additionally, the influence of different substituents on enzyme inhibition activities was assessed to study the structure activity relationships. Molecular docking simulations were performed to rationalize the binding of derivatives/compounds with enzymes. All the synthesized derivatives (1–13 ) were characterized with the aid of spectroscopic instruments such as 1 H-NMR, 13 C-NMR, HR-MS, elemental analysis and FTIR. Communicated by Ramaswamy H. Sarma