Difference between revisions of "Part:BBa K4165182"
 
(4 intermediate revisions by 2 users not shown)
Line 11: Line 11:
  
 
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.
 
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.
 +
 +
===<span class='h3bb'>Sequence and Features</span>===
 +
<partinfo>BBa_K4165182 SequenceAndFeatures</partinfo>
  
 
===Dry Lab Characterization===
 
===Dry Lab Characterization===
Line 17: Line 20:
  
 
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).
 
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).
 +
 +
  
 
<html>
 
<html>
Line 23: Line 28:
  
 
                           Figure 1.: Prediction of 3D structure for Aβ(31–42) peptide.
 
                           Figure 1.: Prediction of 3D structure for Aβ(31–42) peptide.
−
 
−
 
−
<!-- -->
 
−
<span class='h3bb'>Sequence and Features</span>
 
−
<partinfo>BBa_K4165182 SequenceAndFeatures</partinfo>
 
  
  
Line 36: Line 36:
  
 
===References===
 
===References===
 +
 +
Xiong, N., Zhao, Y., Dong, X., Zheng, J., & Sun, Y. (2017). Design of a Molecular Hybrid of Dual Peptide Inhibitors Coupled on AuNPs for Enhanced Inhibition of Amyloid β‐Protein Aggregation and Cytotoxicity. Small, 13(13), 1601666. doi: 10.1002/smll.201601666

Latest revision as of 17:43, 10 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.

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]

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.


References

Xiong, N., Zhao, Y., Dong, X., Zheng, J., & Sun, Y. (2017). Design of a Molecular Hybrid of Dual Peptide Inhibitors Coupled on AuNPs for Enhanced Inhibition of Amyloid β‐Protein Aggregation and Cytotoxicity. Small, 13(13), 1601666. doi: 10.1002/smll.201601666