• Journal of Life Science
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• v.28 no.4
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• pp.408-414
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• 2018

Actein is the well-known active ingredient of Cimicifugae rhizoma (Black cohosh). In this study, we investigated and compared the binding affinity of tubocurarine, actein, and actein derivatives on the B&C domain of the acetylcholine binding protein through in silico computational docking studies. The three-dimensional crystallographic structure of the acetylcholine binding protein B&C domain was obtained from the PDB database (PDB ID: 2XYT). An in silico computational autodocking analysis was performed using PyRx, Autodock Vina, Discovery Studio Version 4.5, and NX-QuickPharm based on scoring functions. The actein showed an optimum binding affinity (docking energy), with the acetylcholine binding protein at -10.50 kcal/mol as compared to the tubocurarine (-9.80 kcal/mol). The interacting amino acids tryptophan 84 and tryptophan 147, in the B domain of the acetylcholine binding protein active site, significantly interacted with the actein and 27-deoxyactein, and (26R)-actein. The centroid XYZ grid position of the tubocurarine was X=38.300689, Y=112.053467, and Z=51.991022, but the actein and its derivatives showed values around X=26.4, Y=127.3, Z=43.7. These results clearly indicated that actein and its derivatives could be a more potent antagonist to the acetylcholine binding protein than tubocurarine. Therefore, the extract of Cimicifugae rhizoma or actein containing biomaterials can substitute for the botulinum toxin-mediated acetylcholine receptor regulation, and be applied to the anti-wrinkle cosmetics industry.