Difference between revisions of "Part:BBa K4165242"

 
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Clamp [2] composed of Seed Binding Peptide Seed ( BBa_K4165007) , linker length of GGSGGGG (BBa_K4165018), Seed Binding Peptide Seed ( BBa_K4165007). Our Clamp design was based on our project aim for binding with Tau and amyloid beta for further degradation.
 
Clamp [2] composed of Seed Binding Peptide Seed ( BBa_K4165007) , linker length of GGSGGGG (BBa_K4165018), Seed Binding Peptide Seed ( BBa_K4165007). Our Clamp design was based on our project aim for binding with Tau and amyloid beta for further degradation.
  
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===Usage and Biology===
 
===Usage and Biology===
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According to Previous Research results, Our binding peptides proved to have dual effect of binding to both Tau and amyloid beta . According to this , we designed our clamps consists of with various linker lengths and peptides parts for further validation of this theory and analysis by wet-lab and dry lab results. According to our project Criteria , our clamps supposed to have binding affinity for tau and amyloid beta higher enough to make the inhibitor (BBa_K4165008) , (BBa_K4165010) unbind from catalytic domain of HTRA1 protease system (BBa_K4165004).
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===3D Modeling and Ranking===
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/2.png" style="margin-left:200px;" alt="" width="500" /></p>
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                          Figure 1. The 3D structure of Clamp [2] modeled by TRrosetta
  
 
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Revision as of 15:39, 8 October 2022


Clamp[2]

Clamp [2] composed of Seed Binding Peptide Seed ( BBa_K4165007) , linker length of GGSGGGG (BBa_K4165018), Seed Binding Peptide Seed ( BBa_K4165007). Our Clamp design was based on our project aim for binding with Tau and amyloid beta for further degradation.

Usage and Biology

According to Previous Research results, Our binding peptides proved to have dual effect of binding to both Tau and amyloid beta . According to this , we designed our clamps consists of with various linker lengths and peptides parts for further validation of this theory and analysis by wet-lab and dry lab results. According to our project Criteria , our clamps supposed to have binding affinity for tau and amyloid beta higher enough to make the inhibitor (BBa_K4165008) , (BBa_K4165010) unbind from catalytic domain of HTRA1 protease system (BBa_K4165004).

3D Modeling and Ranking

                          Figure 1. The 3D structure of Clamp [2] modeled by TRrosetta

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]