Gene fragments of melittin were synthesized according to the sequence of the bee venom gene(melittin) published in Genebank(NM001011607).It was inserted into pGEX6p-1 vector and transferred into BL21(DE3) to induce expression and purify the recombinant protein melittin.The protein concentration was determined,and the molecular weight of the protein expression was analyzed by SDS-PAGE electrophoresis and immune imprinting.In addition,drug sensitivity test and antibacterial test of resistant strains and toxicity test of tumor cells were carried out to determine its biological activity.The recombinant protein showed abvious destination band between 25 and 35 kDa by SDS-PAGE and grayscale analysis.The recombinant protein is highly sensitive to Staphylococcus aureus,moderately sensitive to Escherichia coli,and low sensitive to Pseudomonas aeruginosa and Shigella dysentery.Five concentrations of recombinant proteins 50,25,12.5,6.25 and 3.125 mg/L acted on MCF-7 cells,and stabilized the growth of MCF-7 cells at 12,24,36,48 and 72 h.Compared to the control group,there was a significant difference(P<0.05).Aphidopeptide fusion protein is stable and effective in prokaryotic cells via pGEX6p-1 carrier,and has obvious antibacterial and anti-tumor effects.