Biotechnology Bulletin ›› 2013, Vol. 0 ›› Issue (4): 210-214.

• Research Report • Previous Articles     Next Articles

Study of the Renaturation and Purification of LL-37-haFGF Fusion Protein

Shen Juan1,2, Jin Xiaobao2, Ding Jing2, Zhu Jiayong2   

  1. 1. School of Life Science & Biopharmacology,Guangdong Pharmaceutical University,Guangzhou 510006 ;2. Guangdong Key Laboratory of Pharmaceutical Bioactive Substances,Guangzhou 510006
  • Received:2012-10-28 Revised:2013-04-22 Online:2013-04-22 Published:2013-04-22

Abstract: A new multifunctional healing peptide was designed and developed for the first time, human antimicrobial peptide LL-37 modified haFGF fusion proteins, which can promote healing and fight infection. This paper discussed renaturation conditions and purification conditions of the new fusion protein named recombinant LL-37-haFGF was expressed by Escherichia coli and identified of effects on the refolding of eight kinds of small molecules added to inclusion bodies were preliminary investigated. The result showed supplementation of 0.3 mol/L arginine can greatly improve renaturation efficiency of LL-37-haFGF. The pure product of was obtained with nickel affinity chromatography and CM cation chromatography. Through this study, we obtained 5.9 mg target protein of high purity 95.43%, laying the function for its functional study, and also providing the reference for the preparation of similar multifunctional polypeptide.

Key words: LL-37, haFGF, Fusion protein, Renaturation, Purification