Extraction, Purification and Analysis of Anti cancer activity of Ricin on Colon Cancer Cell Lines and Testing its Efficacy using Insilco Docking

Author Name(s): V. S Prakash Padala
Author Email: prakashpadala6@gmail.com


Ricin, one of the well known plant toxins has played a vital role in the history of medicine. It is usually extracted from Ricinus Communis, a common plant. The use of these proteins in medical treatment since ancient times is reviewed. Later the proteins played important roles in the early days of immunological research and some of the fundamental principles of immunology were discovered with toxic proteins of this group. The present study involves extraction of ricin proteins from powdered castor seed using buffer of definite composition, purification of extracted sample of castor seed was done using Dialysis and Ion Exchange Chromatography. The purified samples were tested for their purification by running sample through 8% SDS PAGE. The anti-cancer activity of ricin proteins were observed on human colon cancer cell lines and further studied the protein-protein docking interactions between the ricin protein and km23, the protein mainly involved in colon cancer. Based upon the docking results it can be analyzed weather the ligand receptor pair used is suitable for docking as favored by their energy values.


Ricinus Communis, Immunological Research, Colon Cancer Cell Lines, Anti Cancer Activity, Docking, Protein Protein Interactions.


Castor belongs to the genus Ricinus of the Euphorbiaceae or spurge family (Atsmon, 1985). Plants range in color from bright red stems and leaves rich in anthocyanin to a uniform dark green. Up to 50% of the dry weight of the seed is oil, with approximately 90% of the fatty acids being ricinoleic acid [1]. Detoxified meal of Ricinus communis can be fed to ruminants or used as a high nitrogen fertilizer due to its inherent properties. Castor oil is estimated to have a market value six times higher than soybean oil [2]. Ricin is a potent plant toxin composed of a 32 kDa A-chain glycoprotein, and a 32 kDa B-chain glycoprotein, linked by a disulfide bond. The A-chain of ricin is a ribosome inactivating protein, preventing protein synthesis by depurinating an adenine residue found in a 28S ribosomal RNA (Olsnes and Pihl, 1982). A single ricin molecule can inactivate over 1500 ribosomes per minute and kill the cell [3]. The B-Chain is a lectin which binds specifically to galactose terminals found on the cell (Olsnes and Pihl, 1973). Binding of the B chain to cell surface receptors triggers endocytosis of the protein (Montfort et al., 1987). Due to these cell inactivating characteristics of ricin it can be employed in the treatment of cancer, wherein inactivating or destroying the surplus cells is needed.

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