Difference between revisions of "Part:BBa K4165194"
 
(3 intermediate revisions by 2 users not shown)
Line 5: Line 5:
 
This part encodes a part of the Amyloid 𝛽 fragment (33-42) which has the ability to bind to A𝛽 plaques inside the brain.
 
This part encodes a part of the Amyloid 𝛽 fragment (33-42) which has the ability to bind to A𝛽 plaques inside the brain.
  
−
<-- Add more about the biology of this part here
 
 
===Usage and Biology===
 
===Usage and Biology===
−
Type of Amyloid-beta binding peptide start from amino acid 33 to 42, this peptide characterized by its solubility which is 134 ± 37 μm.  
+
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 starts from amino acid 33 to 42 of the fibril.
  
−
== Features and codon optimize ==
 
−
This sequence is optimized for E. coli bacteria
 
  
−
==Source==
+
===<span class='h3bb'>Sequence and Features</span>===
−
Homo sapiens Amyloid-beta precursor protein - UniProt (P05067)
+
<partinfo>BBa_K4165194 SequenceAndFeatures</partinfo>
  
−
==References==
 
−
1- Zhao, Y., Cai, J., Liu, Z., Li, Y., Zheng, C., Zheng, Y., ... & Liu, Y. (2018). Nanocomposites inhibit the formation, mitigate the neurotoxicity, and facilitate the removal of β-amyloid aggregates in Alzheimer’s disease mice. Nano letters, 19(2), 674-683.
 
  
−
==Dry lab==
+
===Dry lab===
 
<p style=" font-weight: bold; font-size:14px;"> Modeling </p>
 
<p style=" font-weight: bold; font-size:14px;"> Modeling </p>
−
Due to the nonavailability of a model to this peptide we modeled it in our used modeling software's and after the Running of the quality assessment, the models have been scored to get the top model.
+
The peptide was modeled by several software (Alphafold-Apptest-Pepfold) and the best model was obtained from Apptest.
−
 
+
 
<html>
 
<html>
 
<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/ab-33-42-model.png" style="margin-left:200px;" alt="" width="500" /></p>
 
<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/ab-33-42-model.png" style="margin-left:200px;" alt="" width="500" /></p>
Line 28: Line 22:
 
                                 Figure 1.: Amyloid-beta (33-42) visualized by Pymol.
 
                                 Figure 1.: Amyloid-beta (33-42) visualized by Pymol.
  
−
 
−
 
−
<!-- -->
 
−
<span class='h3bb'>Sequence and Features</span>
 
−
<partinfo>BBa_K4165194 SequenceAndFeatures</partinfo>
 
  
 +
===References===
 +
1- Zhao, Y., Cai, J., Liu, Z., Li, Y., Zheng, C., Zheng, Y., ... & Liu, Y. (2018). Nanocomposites inhibit the formation, mitigate the neurotoxicity, and facilitate the removal of β-amyloid aggregates in Alzheimer’s disease mice. Nano letters, 19(2), 674-683.
  
 
<!-- Uncomment this to enable Functional Parameter display  
 
<!-- Uncomment this to enable Functional Parameter display  

Latest revision as of 19:52, 11 October 2022


Amyloid beta peptide 14 (Aβ 33-42)

This part encodes a part of the Amyloid 𝛽 fragment (33-42) 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 starts from amino acid 33 to 42 of the fibril.


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

Modeling

The peptide was modeled by several software (Alphafold-Apptest-Pepfold) and the best model was obtained from Apptest. 

                                Figure 1.: Amyloid-beta (33-42) visualized by Pymol.


References

1- Zhao, Y., Cai, J., Liu, Z., Li, Y., Zheng, C., Zheng, Y., ... & Liu, Y. (2018). Nanocomposites inhibit the formation, mitigate the neurotoxicity, and facilitate the removal of β-amyloid aggregates in Alzheimer’s disease mice. Nano letters, 19(2), 674-683.