Keywords

Fibronectin, Recombinant Peptide, Tumor Metastasis

Abstract

In order to explore the role of three-domain recombinant fibronectin (fn) in tumor treatment, two three-domain recombinant fn expression plasmids pf94-62 and pf94-82 were constructed, which respectively encode two recombinant polypeptides: ch62 (fn pro1239-ser1515 is connected via met and ala-1690val2049) and ch82 (pro1953-glu1978 with the hepiic end and the N-terminus of the cellii domain deleted from ch62). The engineered bacteria containing the expression plasmid pf94-82 were cultured at 37¡ãC, and ch82 was expressed. The expression product mainly existed in the form of inclusion bodies. After denaturation and renaturation treatment with urea, it was purified by heparin-agarose affinity chromatography. The purified product was subjected to cell culture. Adhesion test. The expression efficiency of ch62 in E. coli is very low (5%), while the expression efficiency of ch82 is very high (21%), suggesting that the N-terminal sequence of the cellii domain in the fn molecule affects the expression of the three-domain recombinant polypeptide in E. coli key structure. Purified ch82 has the function of binding heparin and binding cells, and its ability to bind cells is stronger than that of dual-domain fn. The preparation of ch82 laid the foundation for further research on genetically engineered products with stronger inhibitory effects on tumor metastasis and immune regulation.

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Original research done by Li Mingcai* Feng Zuohua** Li Dong Zhang Guimei

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