Evaluation on the Potential of Ganoderma lucidum Bioactive Compounds as Alpha-Glucosidase Enzyme Inhibitor: A Computational Study

• Published in: Malaysian Journal of Medicine and Health Sciences
• Main Author: Sharif F.; Atan A.K.; Azizan N.H.; Hamid A.A.A.; Ismail C.M.K.H.; Aris M.S.M.
• Format: Article
• Language: English
• Published: Universiti Putra Malaysia Press 2024
• Online Access: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85188672421&doi=10.47836%2fmjmhs.20.2.23&partnerID=40&md5=a85d4a29e9a1cd21e9635d8b93ac30d0

Introduction: Computational simulation study was carried out on bioactive compounds of Ganoderma lucidum (G. lucidum). Methods: Molecular docking and molecular dynamics (MD) simulations were performed. The input files for protein and ligands were retrieved from Protein Data Bank (PDB) and PubChem database. Human maltase-glucoamylase (PDB ID: 3L4Y) is the protein (α-glucosidase enzyme). The ligands are thirteen compounds derived from G. lucidum together with acarbose and miglitol as controls. Results: Docking result showed the lowest binding energy is from Ganomycin B (-7.8 kcal/mol) compared to acarbose and miglitol (-5.0 kcal/mol and -4.4 kcal/mol) respectively. MD simulation showed interaction of 3L4Y-Ganomycin B achieved stable interaction and conformation as follows: root mean square deviation (RMSD) is ± 2.7 Å, average distance of ±1.8 Å and constant hydrogen bonds around 1 - 3. Conclusion: Ganomycin B was found to have good binding affinity, embarking its potential as a potent α-glucosidase inhibitor. © 2024 Universiti Putra Malaysia Press. All rights reserved.