ArticleJournal of cellular and molecular medicine2023
Drug screening of α-amylase inhibitors as candidates for treating diabetes.
Article in Journal of cellular and molecular medicine, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- GC-Ms, UHPLC-MS/MSChemistry & biodiversity · 2026Article
- Chemical Compositions, Traditional Applications, and Biological Activities ofMolecules (Basel, Switzerland) · 2026Review
- Peptides from 'Vaina Morada' Black Bean Inhibit α-Amylase and α-Glucosidase: A Combined In Silico-In Vitro Study.Foods (Basel, Switzerland) · 2025Article
- Antioxidant, Hypotensive, and Antidiabetic Breakthroughs: Bromelain Hydrolysis Unlocks Quinoa's Peptide Potential -Journal of agricultural and food chemistry · 2025Article
- Multiscale Computational and Pharmacophore-Based Screening of ALK Inhibitors with Experimental Validation.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Biochemical evaluation of novel thiazolone derivatives as dual α-glucosidase/α-amylase inhibitors, anti-inflammatory agents.Future medicinal chemistry · 2025Article
- Drug screening of α-amylase inhibitors as candidates for treating diabetes.Journal of cellular and molecular medicine · 2023Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present study, the identification of potential α-amylase inhibitors is explored as a potential strategy for treating type-2 diabetes mellitus. A computationally driven approach using molecular docking was employed to search for new α-amylase inhibitors. The interactions of potential drugs with the enzyme's active site were investigated and compared with the contacts established by acarbose (a reference drug for α-amylase inhibition) in the crystallographic structure 1B2Y. For this active site characterization, both molecular docking and molecular dynamics simulations were performed, and the residues involved in the α-amylase-acarbose complex were considered to analyse the potential drug's interaction with the enzyme. Two potential α-amylase inhibitors (AN-153I105594 and AN-153I104845) have been selected following this computational strategy. Both compounds established a large number of interactions with key binding site α-amylase amino acids and obtained a comparable docking score concerning the reference drug (acarbose). Aiming to further analyse candidates' properties, their ADME (absorption, distribution, metabolism, excretion) parameters, druglikeness, organ toxicity, toxicological endpoints and median lethal dose (LD
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