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Molecules 2011, 16(8), 6243-6254; doi:10.3390/molecules16086243

Anticancer Activity of Chamaejasmine: Effect on Tubulin Protein

1 Department of Rheumatology, The Second Hospital Affiliated Harbin Medical University, Harbin 150086, China 2 Hei longjiang Disabled Federation for Human Care Clinic, Harbin 150020, China These two authors contributed equally to this work.
* Author to whom correspondence should be addressed.
Received: 28 June 2011 / Revised: 15 July 2011 / Accepted: 18 July 2011 / Published: 25 July 2011
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In this work, the anticancer activity of chamaejasmine was studied by evaluating its in vitro cytotoxicity against several human cancer cell lines (MCF-7, A549, SGC-7901, HCT-8, HO-4980, Hela, HepG2, PC-3, LNCap, Vero and MDCK) using the MTT assay. Results indicated chamaejasmine showed more notable anticancer activity than taxol against PC-3 cells, with IC50 values of 2.28 and 3.98 µM, respectively. Furthermore, Western blot analysis showed that chamaejasmine was able to increase the expression of β-tubulin, but not α-tubulin. In silico simulations indicated that chamaejasmine specifically interacts with the active site which is located at the top of β-tubulin, thanks to the presence of strong hydrophobic effects between the core templates and the hydrophobic surface of the TB active site. The binding energy (Einter) was calculated to be −164.77 kcal·mol−1. Results presented here suggest that chamaejasmine possesses anti-cancer properties relating to β-tubulin depolymerization inhibition, and therefore is a potential source of anticancer leads for the pharmaceutical industry.
Keywords: chamaejasmine; anti-cancer activity; PC-3 cells; tubulin; docking chamaejasmine; anti-cancer activity; PC-3 cells; tubulin; docking
This is an open access article distributed under the Creative Commons Attribution License (CC BY) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fang, W.; Liu, S.; Nie, Y. Anticancer Activity of Chamaejasmine: Effect on Tubulin Protein. Molecules 2011, 16, 6243-6254.

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