Molecular docking study on columbin isolated from Tinospora cordifolia as a cholinesterase inhibitor


 Purpose: To investigate the acetylcholinesterase (AChE) inhibitory potential of columbin and also to assess its binding affinity against AChE protein.
 Methods: Crystals were isolated from ethyl acetate fraction Tinospora cordifolia using column chromatography structure was determined x-ray crystallography. Ellman colorimetric assay used determine effect in vitro while molecular docking performed MOE 2015.010 software. The selected protein data bank (PDB) modeled PDB ID: 10CE (pacific electric ray).
 Results: crystal refinement were: C20H22O6, Orthorhombic, P212121, a = 7.4951(2) Å (α 90°), b 11.6451(3) (β c 19.5882(5) (γ V=1709.68(8) Å3, Z 4, Density (calculated) 1.392 Mg/m3, absorption coefficient 0.851 mm-1, goodness-of-fit on F2 =1.091, T 100(2) K. Columbin demonstrated good with half-maximal concentration (IC50) 1.2993 ± 0.17 mg/mL. Molecular revealed that it exhibited hydrophobic hydrogen bonding interactions surrounding residues, this accelerated complexation between ligands active site enzyme.
 Conclusion: may be useful management neurodegenerative conditions such as Alzheimer’s disease.