Difference between revisions of "Part:BBa K5302003"
 
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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.
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__NOTOC__
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<partinfo>BBa_K5302003 short</partinfo>
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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. 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 pBBR1MCS-2 plasmid as a backbone and transfered ZVEGF into Escherichia coli Nissle 1917, and finally succeeded in expressing ZVEGF.
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<html>
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<div style="text-align:center;">
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    <img src="https://static.igem.wiki/teams/5302/images/part-registry-v107-5.png"
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        width="60%" style="display:block; margin:auto;" alt="Jamboree Program" >
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    <div style="text-align:center;">
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        <caption>
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            <b>Figure 1. </b> ZVEGF sequence
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        </caption>
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    </div>
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</div>
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<html>
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<div style="text-align:center;">
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    <img src="https://static.igem.wiki/teams/5302/images/part-registry-v107-6.png"
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        width="60%" style="display:block; margin:auto;" alt="Jamboree Program" >
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    <div style="text-align:center;">
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        <caption>
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            <b>Figure 2. </b> VEGF-binding site of ZVEGF
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        </caption>
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    </div>
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<html>
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<div style="text-align:center;">
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    <img src="https://static.igem.wiki/teams/5302/images/part-registry-v107-7.png"
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        width="60%" style="display:block; margin:auto;" alt="Jamboree Program" >
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    <div style="text-align:center;">
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        <caption>
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            <b>Figure 3. </b> Colony PCR results of pBBR-OmpA-ZVEGF
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        </caption>
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    </div>
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<!-- Add more about the biology of this part here
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===Usage and Biology===
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K5302003 SequenceAndFeatures</partinfo>
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<!-- Uncomment this to enable Functional Parameter display
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===Functional Parameters===
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<partinfo>BBa_K5302003 parameters</partinfo>
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Latest revision as of 02:59, 2 October 2024


ZVEGF

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. 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 pBBR1MCS-2 plasmid as a backbone and transfered ZVEGF into Escherichia coli Nissle 1917, and finally succeeded in expressing ZVEGF.

Jamboree Program
Figure 1. ZVEGF sequence

Jamboree Program
Figure 2. VEGF-binding site of ZVEGF

Jamboree Program
Figure 3. Colony PCR results of pBBR-OmpA-ZVEGF

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]