Difference between revisions of "Part:BBa K5302006"
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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.V114 has been identified as a small potent VEGF-binding peptide, which is composed of 8 amino acids--- that is VEPNc[CDIHVnLWEWEC]FERL, and there is a disulfide bond between N and F, making the stucture more stable. This peptide has a similiar structure and VEGF-binding site as V107, and it shows great affinity with VEGF(Kd=0.11 μM). We used pBBR1MCS-2 plasmid as a backbone and transfered V114 into Escherichia coli Nissle 1917, and finally succeeded in expressing V114. | 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.V114 has been identified as a small potent VEGF-binding peptide, which is composed of 8 amino acids--- that is VEPNc[CDIHVnLWEWEC]FERL, and there is a disulfide bond between N and F, making the stucture more stable. This peptide has a similiar structure and VEGF-binding site as V107, and it shows great affinity with VEGF(Kd=0.11 μM). We used pBBR1MCS-2 plasmid as a backbone and transfered V114 into Escherichia coli Nissle 1917, and finally succeeded in expressing V114. | ||
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
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===Functional Parameters=== | ===Functional Parameters=== | ||
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Revision as of 04:34, 1 October 2024
V114
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.V114 has been identified as a small potent VEGF-binding peptide, which is composed of 8 amino acids--- that is VEPNc[CDIHVnLWEWEC]FERL, and there is a disulfide bond between N and F, making the stucture more stable. This peptide has a similiar structure and VEGF-binding site as V107, and it shows great affinity with VEGF(Kd=0.11 μM). We used pBBR1MCS-2 plasmid as a backbone and transfered V114 into Escherichia coli Nissle 1917, and finally succeeded in expressing V114.
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]