Difference between revisions of "Part:BBa K5302004"
 
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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. Z3C is derived from three helix 58-residue Z-domain of staphylococcal protein A, but it has three helix. Z3C also shows great affinity with VEGF(KD=41 nM). We used pBBR plasmid as a backbone and transfered Z3C into Escherichia coli Nissle 1917, and finally succeeded in expressing Z3C.
 
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. Z3C is derived from three helix 58-residue Z-domain of staphylococcal protein A, but it has three helix. Z3C also shows great affinity with VEGF(KD=41 nM). We used pBBR plasmid as a backbone and transfered Z3C into Escherichia coli Nissle 1917, and finally succeeded in expressing Z3C.
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    <img src="https://static.igem.wiki/teams/5302/images/part-registry-z3c-1.png"
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        width="60%" style="display:block; margin:auto;" alt="Jamboree Program" >
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        <caption>
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            <b>Figure 1. </b> sequence of Z3C and its KD with VEGF
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    <img src="https://static.igem.wiki/teams/5302/images/part-registry-z3c-2.png"
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        width="60%" style="display:block; margin:auto;" alt="Jamboree Program" >
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        <caption>
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            <b>Figure 2. </b> Cartoon representation of the crystal structure of the mini-Z highlighting randomized residues shown as sticks and coloring the helices
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    <img src="https://static.igem.wiki/teams/5302/images/part-registry-z3c-3.png"
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        width="60%" style="display:block; margin:auto;" alt="Jamboree Program" >
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        <caption>
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            <b>Figure 3. </b> Colony PCR results of pBBR-OmpA-Z3C
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    <img src="https://static.igem.wiki/teams/5302/images/part-registry-z3c-4.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 4. </b> SDS-PAGE analysis of pBBR1MCS-OmpA-Z3C expression in Escherichia coli Nissle 1917 (1)
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        </caption>
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    <img src="https://static.igem.wiki/teams/5302/images/part-registry-z3c-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 5. </b> SDS-PAGE analysis of pBBR1MCS-OmpA-Z3C expression in Escherichia coli Nissle 1917 (2)
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        </caption>
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<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Latest revision as of 08:37, 1 October 2024


Z3C

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. Z3C is derived from three helix 58-residue Z-domain of staphylococcal protein A, but it has three helix. Z3C also shows great affinity with VEGF(KD=41 nM). We used pBBR plasmid as a backbone and transfered Z3C into Escherichia coli Nissle 1917, and finally succeeded in expressing Z3C.

Jamboree Program
Figure 1. sequence of Z3C and its KD with VEGF

Jamboree Program
Figure 2. Cartoon representation of the crystal structure of the mini-Z highlighting randomized residues shown as sticks and coloring the helices

Jamboree Program
Figure 3. Colony PCR results of pBBR-OmpA-Z3C

Jamboree Program
Figure 4. SDS-PAGE analysis of pBBR1MCS-OmpA-Z3C expression in Escherichia coli Nissle 1917 (1)

Jamboree Program
Figure 5. SDS-PAGE analysis of pBBR1MCS-OmpA-Z3C expression in Escherichia coli Nissle 1917 (2)

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]