Open Access
Open access
Molecules, volume 29, issue 23, pages 5599

Novel Benzimidazole-Endowed Chalcones as α-Glucosidase and α-Amylase Inhibitors: An Insight into Structural and Computational Studies

Prashasthi V. Rai 1
Ramith Ramu 2
P Akhileshwari 3
Sudharshan Prabhu 4
Nupura Manish Prabhune 4
P V Deepthi 5
P T Anjana 6
Ganavi D 7
A. M. Vijesh 8
Khang Wen Goh 9
Mohammad Z Ahmed 10
Vasantha Kumar 1, 11
Show full list: 12 authors
Publication typeJournal Article
Publication date2024-11-27
Journal: Molecules
scimago Q1
SJR0.744
CiteScore7.4
Impact factor4.2
ISSN14203049
Abstract

In search of novel antidiabetic agents, we synthesized a new series of chalcones with benzimidazole scaffolds by an efficient ‘one-pot’ nitro reductive cyclization method and evaluated their α-glucosidase and α-amylase inhibition studies. The ‘one-pot’ nitro reductive cyclization method offered a simple route for the preparation of benzimidazoles with excellent yield and higher purity compared to the other conventional acid- or base-catalyzed cyclization methods. 1H, 13C NMR, IR, and mass spectrum data were used to characterize the compounds. Single-crystal XRD data confirmed the 3D structure of compound 7c, which was crystalized in the P1¯ space group of the triclinic crystal system. Hirshfeld surface analysis validates the presence of O-H..O, O-H…N, and C-H…O intermolecular hydrogen bonds. From the DFT calculations, the energy gap between the frontier molecular orbitals in 7c was found to be 3.791 eV. From the series, compound 7l emerged as a potent antidiabetic agent with IC50 = 22.45 ± 0.36 µg/mL and 20.47 ± 0.60 µg/mL against α-glucosidase and α-amylase enzymes, respectively. The in silico molecular docking studies revealed that compound 7l has strong binding interactions with α-glucosidase and α-amylase proteins. Molecular dynamics studies also revealed the stability of compound 7l with α-glucosidase and α-amylase proteins.

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