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March 22, 2026Current Enzyme Inhibition

Design, Synthesis, and In Vitro Evaluation of Triazole-enamine Derivatives for Antidiabetic Activity: α-Amylase Inhibition and Computational Investigations

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Authors

VPV. ParthasarathiHKHemalatha K

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Overview

In vitro evaluation examines α-amylase inhibition by triazole derivatives, suggesting promising antidiabetic agents.

Key Points

  • This research aims to develop and assess the antidiabetic activity of triazole-enamine derivatives through α-amylase inhibition.
  • Synthesis of triazole derivatives (PT1–PT14) and structural confirmation
  • Molecular docking studies to evaluate binding to α-amylase
  • In vitro assays to determine IC50 values for enzyme inhibition
  • Prediction of ADME properties including Lipinski’s compliance
  • Molecular docking showed binding affinities ranging from –6.9 to –8.4 kcal/mol with PT13 having the strongest affinity
  • PT13 was identified as the most potent inhibitor with an IC50 of 40.0 ± 0.01 μM
  • PT14 and PT9 followed with IC50 values of 43.1 ± 0.25 μM and 45.4 ± 0.08 μM respectively
  • Predictions indicated high gastrointestinal absorption and favorable Lipinski compliance

Cite This Study

Parthasarathi et al. (2026) studied this question.

synapsesocial.com/papers/69bf899af665edcd009e966ahttps://doi.org/10.2174/0115734080423154251203122430
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

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