David Stephen, A (2021) Binding studies of known molecules with acetylcholinesterase and bovine serum albumin: A comparative view. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. pp. 1-14. ISSN 1386-1425

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The interactions between selected molecules (piperine, tacrine, curcumin and silibinin) and proteins (acetylcholinesterase and bovine serum albumin) were investigated by Fluorescence spectroscopy, molecular docking, molecular dynamics, free energy calculation and non-covalent interaction analysis. These binding characteristics are of huge interest for understanding pharmacokinetic mechanism of the target molecules. The steady-state emission spectrum results showed that presence of static quenching mode for piperine, tacrine, curcumin, silibinin molecules with BSA and AChE complexes separately
and this excitation-emission matrix analysis suggest that formation of ground-state complex between piperine, tacrine, curcumin, silibinin drugs and both BSA, AChE protein molecules. And, the binding
model from molecular docking analysis of both BSA and AChE with these molecules clearly displayed
non-covalent interactions (hydrogen bonding and hydrophobic interactions) which played a significant
role in the binding mechanism. Further, the protein-ligand complexes are subjected to molecular dynamics and binding free energy calculation to confirm the stability of the molecule in the active site of BSA
and AChE. The NCI (non-covalent interaction) approach supports to visualize the iso-surface of the
reduced density gradient of such interactions between protein and ligands.

Item Type: Article
Uncontrolled Keywords: Interaction study Steady-state spectroscopy analysis Molecular docking MD simulation and binding Free energy NCI analysis
Divisions: PSG College of Arts and Science > Department of Physics
Depositing User: Mr Team Mosys
Date Deposited: 29 Jun 2022 10:47
Last Modified: 29 Jun 2022 10:47
URI: http://ir.psgcas.ac.in/id/eprint/1272

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