Part:BBa_K5302003

ZVEGF is a 59-residue three-helix peptide that was developed by Fedorova et al. by randomizing 9 residues on helices 1 and 2 of the Z-domain scaffold via phage display, followed by selection for binding to the VEGF8-109 dimer. A co-crystal structure of ZVEGF with VEGF8-109 shows that the engineered Z-domain adopts the expected three-helix bundle tertiary structure and engages the receptor-recognition sites on the VEGF dimer through a surface formed by helices 1 and 2 of ZVEGF. It shows great affinity with VEGF(Ki=0.41 μM).We used pBBR plasmid as a backbone and transfered ZVEGF into Escherichia coli Nissle 1917, and finally succeeded in expressing ZVEGF.