Fusion Protein on Sumo Molecular Chaperone and Antifungal Peptide Drs Help to Soluble Expression
Sumo分子伴侣与富含二硫键的抗真菌肽Drs基因的融合有助于其可溶性表达

After Sumo molecular chaperone and antifungal peptide Drosomycin were synthesized by PCR,the recombinant plasmid pET-3c-SD was constructed successfully.After the recombinant plasmid was transformed into BL21(DE3),fusion proteins expressed in the E.coli 21(DE3)by the induction of IPTG.Target proteins attained 80 percent in total proteins.Meantime,Soluble protein exceeds 80% in total target proteins.The fusion protein was purified by Ni-NTA affinity chromatography,and its purification exceeds 95 percent.The experiment shows the fusion protein own the antifungal activity,and this construction strategy help to facilitate small molecular peptide expression that had several two disulfide bonds.