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Design of Novel Benzimidazole-Propane Hydrazide Derivatives As Α-Glucosidase and Α-Amylase Inhibitors: In Vitro and in Silico Studies Publisher



Mohammadizadeh S1 ; Karimian S2 ; Dastyafteh N3 ; Noori M3 ; Doraghi F3 ; Mohammadikhanaposhtani M4 ; Larijani B3 ; Mahdavi M3 ; Sadeghian N5 ; Aktas A6 ; Taslimi P5 ; Gulcin I7
Authors
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Authors Affiliations
  1. 1. Digestive Diseases Research Center, Digestive Diseases Research Institute, Shariati Hospital, Tehran University of Medical sciences, Tehran, Iran
  2. 2. Medicinal and Natural Products Chemistry Research Center, Shiraz University of Medical Sciences, Shiraz, Iran
  3. 3. Endocrinology and Metabolism Research Center, Endocrinology and Metabolism Clinical Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran
  4. 4. Cellular and Molecular Biology Research Center, Health Research Institute, Babol University of Medical Sciences, Babol, Iran
  5. 5. Department of Biotechnology, Faculty of Science, Bartin University, Bartin, 74110, Turkey
  6. 6. Inonu University, Vocational School of Health Service, Malatya, 44280, Turkey
  7. 7. Department of Chemistry, Faculty of Science, Ataturk University, Erzurum, Turkey

Source: Medicinal Chemistry Research Published:2025


Abstract

A new series of benzimidazole-propane hydrazide derivatives 9a-k were designed, synthesized, and evaluated for their inhibition ability against α-glucosidase and α-amylase. The results of the in vitro evaluations showed that all the tested compounds exhibited significant inhibition against α-glucosidase and α-amylase. Title compounds 9a-k exhibited varying degrees of inhibitory ability against α-glucosidase, with IC50 values in the range of 73.86–151.54 nM, in comparison to the standard acarbose drug with IC50 value of 174.50 nM. Similarly, these compounds demonstrated varying degrees of α-amylase inhibitory ability (the IC50 values ranged from 42.50 to 78.58 nM in comparison to acarbose with IC50 of 79.05 nM). Among the synthesized compounds, compound 9 h demonstrated the highest α-glucosidase inhibitory activity and compound 9 f demonstrated the highest anti-α-amylase activity. To further investigation on the potential of these derivatives as α-glucosidase and α-amylase inhibitors, molecular docking were conducted on all the synthesized compounds 9a-k. Docking results were in agreement with in vitro results. Molecular dynamics of compound 9 h showed that complex compound 9h-α-glucosidase had acceptable stability and flexibility. Calculations of physicochemical properties of compound 9a-k showed that these compounds fallowed of the main drug-likeness rules. Furthermore, the prediction of pharmacokinetics and toxicity profiles of compound 9 h showed that this compound can be considered as a lead drug structure. (Figure presented.) © The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2024.
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