Difference between revisions of "Part:BBa K4165193"
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===Usage and Biology=== | ===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 acids 32 to 42 of the fibril. | |
===<span class='h3bb'>Sequence and Features</span>=== | ===<span class='h3bb'>Sequence and Features</span>=== | ||
<partinfo>BBa_K4165193 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4165193 SequenceAndFeatures</partinfo> | ||
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===Dry lab=== | ===Dry lab=== | ||
<p style=" font-weight: bold; font-size:14px;"> Modeling </p> | <p style=" font-weight: bold; font-size:14px;"> Modeling </p> | ||
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+ | The peptide was modeled by several software (Alphafold-Apptest-Pepfold) and the best model from Apptest scored 3 out of 6 according to our Quality assessment code. | ||
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Latest revision as of 19:40, 11 October 2022
Amyloid beta peptide 13 (Aβ 32-42)
This part encodes a part of the Amyloid 𝛽 fragment (32-42) 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 acids 32 to 42 of the fibril.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Dry lab
Modeling
The peptide was modeled by several software (Alphafold-Apptest-Pepfold) and the best model from Apptest scored 3 out of 6 according to our Quality assessment code.
Figure 1.: Amyloid-beta (32-42) top model 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.