Difference between revisions of "Part:BBa K5302010"
 
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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.
 
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).
 
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).
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    <img src="https://static.igem.wiki/teams/5302/images/part-registry-vegfr-mask-vgb-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> structure of VGB
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    </div>
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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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Latest revision as of 13:10, 1 October 2024


VGB

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
    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]