Difference between revisions of "Part:BBa K5302005"
| Line 1: | Line 1: | ||
| − | + | 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. | ||
Revision as of 04:21, 1 October 2024
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.