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  3. Chalcone Scaffolds Exhibiting Acetylcholinesterase Enzyme Inhibition: Mechanistic and Computational Investigations

Chalcone Scaffolds Exhibiting Acetylcholinesterase Enzyme Inhibition: Mechanistic and Computational Investigations

  • Molecules. 2022 May 16;27(10):3181. doi: 10.3390/molecules27103181.
Yossra A Malik 1 2,  Talal Ahmed Awad 1 3,  Mohnad Abdalla 4,  Sakina Yagi 5,  Hassan A Alhazmi 6 7,  Waquar Ahsan 7,  Mohammed Albratty 7,  Asim Najmi 7,  Shabbir Muhammad 8,  Asaad Khalid 1 6
Affiliations

Affiliations

  • 1 Department of Biochemistry, Medicinal and Aromatic Plants and Traditional Medicine Research Institute, National Center for Research, Khartoum 11111, Sudan.
  • 2 Unit of Molecular Genetics, Central Laboratory, Khartoum 11111, Sudan.
  • 3 Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Ibn Sina University, Khartoum 10995, Sudan.
  • 4 Key Laboratory of Chemical Biology (Ministry of Education), Department of Pharmaceutics, School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, 44 Cultural West Road, Jinan 250012, China.
  • 5 Department of Botany, Faculty of Science, University of Khartoum, Khartoum 11115, Sudan.
  • 6 Substance Abuse and Toxicology Research Center, Jazan University, P.O. Box 114, Jazan 45142, Saudi Arabia.
  • 7 Department of Pharmaceutical Chemistry, College of Pharmacy, Jazan University, P.O. Box 114, Jazan 45142, Saudi Arabia.
  • 8 Department of Chemistry, College of Science, King Khalid University, P.O. Box 9004, Abha 61413, Saudi Arabia.
PMID: 35630658 DOI: 10.3390/molecules27103181
Abstract

This study was aimed to perform the mechanistic investigations of chalcone scaffold as inhibitors of acetylcholinesterase (AChE) Enzyme using molecular docking and molecular dynamics simulation tools. Basic Chalcones (C1-C5) were synthesized and their in vitro AChE inhibition was tested. Binding interactions were studied using AutoDock and Surflex-Dock programs, whereas the molecular dynamics simulation studies were performed to check the stability of the ligand-protein complex. Good AChE inhibition (IC50 = 22 ± 2.8 to 37.6 ± 0.75 μM) in correlation with the in silico results (binding energies = -8.55 to -8.14 Kcal/mol) were obtained. The mechanistic studies showed that all of the functionalities present in the chalcone scaffold were involved in binding with the amino acid residues at the binding site through hydrogen bonding, π-π, π-cation, π-sigma, and hydrophobic interactions. Molecular dynamics simulation studies showed the formation of stable complex between the AChE Enzyme and C4 ligand.

Keywords

acetylcholinesterase inhibitors; chalcones; in silico; mechanistic; molecular docking; molecular dynamics simulations.

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