Difference between revisions of "Part:BBa K4165182"

 
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This part encodes a part of the Amyloid 𝛽 fragment (31-42) which has the ability to bind to A𝛽 plaques inside the brain.
 
This part encodes a part of the Amyloid 𝛽 fragment (31-42) which has the ability to bind to A𝛽 plaques inside the brain.
  
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===Usage and Biology===
 
===Usage and Biology===
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Segments of amyloid beta fibrils are widely used as a recognition sequence for amyloid beta plaques inside the brain, this is due to the homotypic interactions in the C-terminus of fibrils.
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This peptide was proved to completely eliminate neurotoxicity of plaques when tested in vivo, this is due to the hydrophobic interactions between peptide and Aβ oligomers, followed by the formation of non-toxic oligomers.
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===Dry Lab Characterization===
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<p style=" font-weight: bold; font-size:14px;"> Modeling </p>
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For the prediction of 3D structure, the peptide was modeled through three peptide modeling software (Apptest, Alphafold2, and Pepfold3) followed by ranking them according to our pipeline parameters. Various models for this peptide ranked 6 out of 6, with the top-ranked model being (Apptest model 77).
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/ab3142.png" style="margin-left:200px;" alt="" width="500" /></p>
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                          Figure 1.: Prediction of 3D structure for Aβ(31–42) peptide.
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<partinfo>BBa_K4165182 parameters</partinfo>
 
<partinfo>BBa_K4165182 parameters</partinfo>
 
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===References===

Revision as of 13:05, 6 October 2022


Amyloid Beta Peptide 2 (Aβ 31-42)

This part encodes a part of the Amyloid 𝛽 fragment (31-42) which has the ability to bind to A𝛽 plaques inside the brain.


Usage and Biology

Segments of amyloid beta fibrils are widely used as a recognition sequence for amyloid beta plaques inside the brain, this is due to the homotypic interactions in the C-terminus of fibrils.

This peptide was proved to completely eliminate neurotoxicity of plaques when tested in vivo, this is due to the hydrophobic interactions between peptide and Aβ oligomers, followed by the formation of non-toxic oligomers.

Dry Lab Characterization

Modeling

For the prediction of 3D structure, the peptide was modeled through three peptide modeling software (Apptest, Alphafold2, and Pepfold3) followed by ranking them according to our pipeline parameters. Various models for this peptide ranked 6 out of 6, with the top-ranked model being (Apptest model 77). 

                          Figure 1.: Prediction of 3D structure for Aβ(31–42) peptide.


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]


References