Difference between revisions of "Part:BBa K5302043"

 
 
Line 4: Line 4:
  
 
This work is derived from pBBR-INP-VEGFR1D2 and pUC19-VGB, and it has undergone codon optimization. This composite part combines INP(about 30kda) and VEGFR1D2(approximately 12kda), and it adds a fragment as a mask. We succeeded in transferring this plasmid into Escherichia coli Nissle 1917 and let it express VEGFR1D2. The plasmid uses lac promotor and has kanamycin resistence.
 
This work is derived from pBBR-INP-VEGFR1D2 and pUC19-VGB, and it has undergone codon optimization. This composite part combines INP(about 30kda) and VEGFR1D2(approximately 12kda), and it adds a fragment as a mask. We succeeded in transferring this plasmid into Escherichia coli Nissle 1917 and let it express VEGFR1D2. The plasmid uses lac promotor and has kanamycin resistence.
 +
 +
<hr>
 +
 +
This part is a cyclic peptide (known as VGB1) reproducing the α1 helix and its adjacent region based on the X-ray structure of VEGF-B/VEGFR1D2, he sequence of the designed 17-amino acid peptide (referred to as VGB1) was 2HN-CSWIDVYTRATCQPRPL-COOH. It exhibits high affinity for VEGFR-like receptors, allowing it to effectively compete with VEGF for binding to VEGFR. Consequently, this peptide has been utilized as a masking agent. Upon administration into the human body, it preemptively binds to VEGFR, preventing VEGF from engaging with the receptor.
 +
Given that matrix metalloproteinases (MMPs) are present at high concentrations in the tumor microenvironment (TME), they can degrade this VEGFR-masking peptide (designated as #29). This degradation allows VEGF to subsequently bind to the VEGFR-like receptors, triggering their activation. Therefore, this peptide functions as a biological switch, becoming active when exposed to the TME upon the entry of engineered chimeric nanoparticles ( Escherichia coli Nissle 1917).
 +
 +
<html>
 +
<div style="text-align:center;">
 +
    <img src="https://static.igem.wiki/teams/5302/images/part-registry-vegfr-mask-vgb-1.png"
 +
        width="60%" style="display:block; margin:auto;" alt="Jamboree Program" >
 +
    <div style="text-align:center;">
 +
        <caption>
 +
            <b>Figure 1. </b> structure of VGB
 +
        </caption>
 +
    </div>
 +
</div>
 +
</html>
 +
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Latest revision as of 02:50, 2 October 2024


pBBR-INP-l2VGB

This work is derived from pBBR-INP-VEGFR1D2 and pUC19-VGB, and it has undergone codon optimization. This composite part combines INP(about 30kda) and VEGFR1D2(approximately 12kda), and it adds a fragment as a mask. We succeeded in transferring this plasmid into Escherichia coli Nissle 1917 and let it express VEGFR1D2. The plasmid uses lac promotor and has kanamycin resistence.

This part is a cyclic peptide (known as VGB1) reproducing the α1 helix and its adjacent region based on the X-ray structure of VEGF-B/VEGFR1D2, he sequence of the designed 17-amino acid peptide (referred to as VGB1) was 2HN-CSWIDVYTRATCQPRPL-COOH. It exhibits high affinity for VEGFR-like receptors, allowing it to effectively compete with VEGF for binding to VEGFR. Consequently, this peptide has been utilized as a masking agent. Upon administration into the human body, it preemptively binds to VEGFR, preventing VEGF from engaging with the receptor. Given that matrix metalloproteinases (MMPs) are present at high concentrations in the tumor microenvironment (TME), they can degrade this VEGFR-masking peptide (designated as #29). This degradation allows VEGF to subsequently bind to the VEGFR-like receptors, triggering their activation. Therefore, this peptide functions as a biological switch, becoming active when exposed to the TME upon the entry of engineered chimeric nanoparticles ( Escherichia coli Nissle 1917).

Jamboree Program
Figure 1. structure of VGB


Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal EcoRI site found at 4617
    Illegal XbaI site found at 3189
    Illegal PstI site found at 2016
    Illegal PstI site found at 3177
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal EcoRI site found at 4617
    Illegal PstI site found at 2016
    Illegal PstI site found at 3177
    Illegal NotI site found at 1057
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal EcoRI site found at 4617
    Illegal BglII site found at 1803
    Illegal BamHI site found at 3195
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal EcoRI site found at 4617
    Illegal XbaI site found at 3189
    Illegal PstI site found at 2016
    Illegal PstI site found at 3177
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal EcoRI site found at 4617
    Illegal XbaI site found at 3189
    Illegal PstI site found at 2016
    Illegal PstI site found at 3177
    Illegal NgoMIV site found at 2467
    Illegal NgoMIV site found at 2750
    Illegal NgoMIV site found at 3616
    Illegal NgoMIV site found at 5282
    Illegal AgeI site found at 4193
    Illegal AgeI site found at 5122
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 1379
    Illegal SapI.rc site found at 2316
    Illegal SapI.rc site found at 2526