Part:BBa_K5302005
miniZ
This year, the USTC iGEM team has utilized the competitive binding of vascular endothelial growth factor (VEGF) to develop a targeted bacterial therapy for solid tumors. Our quest for the optimal VEGF-binding protein(or peptide) led us to an in-depth exploration of proteins structurally akin to the vascular endothelial growth factor receptor (VEGFR), which we have named VEGFR-like. This part is derived from three helix 58-residue Z-domain of staphylococcal protein A. And through stabilizing mutations and the addition of a disulfide constraint the Z-domain is reengineered into a two-helix 34-residue “mini-Z” version that retains the parent's affinity. This is supposed to be more potent binders against VEGF. We used pBBR1MCS-2 plasmid as a backbone and transfered miniZ into Escherichia coli Nissle 1917, and finally succeeded in expressing miniZ.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
biology | Escherichia coli Nissle 1917 |