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Design and Evaluation of Indole-Based Schiff Bases as α-Glucosidase Inhibitors: CNN-Enhanced Docking, MD Simulations, ADMET Profiling, and SAR Analysis

  • Seema K. Bhagwat
    ,
  • Sachin V. Patil
    ,
  • Abraham Vidal-Limon
    ,
  • J. Oscar C. Jimenez-Halla
    ,
  • Balasaheb K. Ghotekar
    ,
  • Vivek D. Bobade
*Corresponding author for this work
  • Research Centre HPT Arts and RYK Science College (Affiliated to Savitribai Phule Pune University)
    ,
  • Instituto de Ecologia, A.C.
    ,
  • Universidad de Guanajuato
    ,
  • Tecnológico Nacional de México, Mexico City
    ,
  • Universidad Veracruzana
    ,
Research Output:
Contribution to journal
Article
Peer-review

Open access

Publication Information

Output type

Research Output:
Contribution to journal
Article
Peer-review

Original language

English

Article number

3651

Journal (Volume, Issue Number)

Molecules (Volume 30, Issue 17)

Publication milestones

  • Published - 08/09/2025

Publication status

Published - 08/09/2025

Publication IDs

  • Scopus: 105015594274
  • PubMed: 40942175

Abstract

Type 2 diabetes mellitus (T2DM) remains a global health challenge, prompting the development of novel α-glucosidase inhibitors (AGIs) to regulate postprandial hyperglycemia. This study reports the design, synthesis, and evaluation of indole-based Schiff base derivatives (4a–j) bearing a fixed methoxy group at the C5 position. This substitution was strategically introduced to enhance lipophilicity, electronic delocalization, and π-stacking within the enzyme active site. Among the series, compound 4g (3-bromophenyl) exhibited the highest inhibitory activity (IC50 = 10.89 µM), outperforming the clinical reference acarbose (IC50 = 48.95 µM). The mechanism was supported by in silico analyses, such as the Density Functional Theory (DFT), molecular electrostatic potential (MEP) mapping, and molecular dynamics simulations, and CNN-based docking revealed that 4g engages in stable hydrogen bonding and π–π interactions with key residues (Asp327, Asp542, and Phe649), suggesting a potent and selective mode of inhibition. In silico ADMET predictions indicated favorable pharmacokinetic properties. Together, these results establish C5–methoxy substitution as a viable strategy to enhance α-glucosidase inhibition in indole-based scaffolds.

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