Fusion with pep-1, a cell-penetrating peptide, enhances the transmembrane ability of human epidermal growth factor

Here, human epidermal growth factor (hEGF) was fused with glutathione S-transferase (GST) and Pep-1, the first commercial cell-penetrating peptide, in Escherichia coli . The fusion protein was firstly purified with the affinity chromatography, and then the GST tag was released by TEV protease.

Final purification was achieved by the ion exchange chromatography. The biological activities and the transmembrane ability of the obtained products were determined using scratch wound-healing assay, MTT analysis, and immunofluorescence assay. The results showed that both rhEGF and Pep-1-fused hEGF were soluble expressed in E. coli .