Novel Benzimidazole-Endowed Chalcones as α-Glucosidase and α-Amylase Inhibitors: An Insight into Structural and Computational Studies
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 si...
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| Main Authors: | , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-11-01
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| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/29/23/5599 |
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| Summary: | 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. <sup>1</sup>H, <sup>13</sup>C NMR, IR, and mass spectrum data were used to characterize the compounds. Single-crystal XRD data confirmed the 3D structure of compound <b>7c,</b> which was crystalized in the P<inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mover accent="true"><mn>1</mn><mo>¯</mo></mover></semantics></math></inline-formula> 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 <b>7c</b> was found to be 3.791 eV. From the series, compound <b>7l</b> emerged as a potent antidiabetic agent with IC<sub>50</sub> = 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 <b>7l</b> has strong binding interactions with α-glucosidase and α-amylase proteins. Molecular dynamics studies also revealed the stability of compound <b>7l</b> with α-glucosidase and α-amylase proteins. |
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| ISSN: | 1420-3049 |