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YUAN Feng-rui, ZHANG Min-jing, TONG Lei, SU Zhi-jian, XIANG Qi, HUANG Ya-dong. Expression,purification and activity assay of SUMO-HBD2-4D5 fusion protein[J]. Journal of China Pharmaceutical University, 2011, 42(3): 266-271.
Citation: YUAN Feng-rui, ZHANG Min-jing, TONG Lei, SU Zhi-jian, XIANG Qi, HUANG Ya-dong. Expression,purification and activity assay of SUMO-HBD2-4D5 fusion protein[J]. Journal of China Pharmaceutical University, 2011, 42(3): 266-271.
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Expression,purification and activity assay of SUMO-HBD2-4D5 fusion protein

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  • Human beta defensin 2 (HBD2) is a small antimicrobial peptide,which is able to inhibit the proliferation of multiple cancer cells.In this study,HBD2 was linked to a single chain of the Her-2 antibody fragment (4D5 scFv) by genetic engineering,and the soluble HBD2-4D5 was expressed successfully by the small ubiquitin-like modifier (SUMO）molecular chaperones in E.coli.HBD-4D5 was purified using the combination of Ni-NTA Sepharose FF,digestion by specific SUMO protease and Sephadex G-25,the purity was higher than 95% with a yield of 15 mg/L. The fusion HBD2-4D5 showed significant antibacterial activity against E.coliK12D31 andStaphylococcus aureus (ATCC25923), suggesting that the activity of HBD2 was reserved. Also, HBD2-4D5 demonstrated selective binding activity to SK-BR-3, a Her-2 over expressed breast cancer cell line. This finding provides foundations for further investigation for the treatment of the HER-2 over expressed breast cancer.
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