Difference between revisions of "Part:BBa K4165152"
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Tau binding peptide targeting the PHF seed of Tau | Tau binding peptide targeting the PHF seed of Tau | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
ISAD1 peptide with amino acid sequence of SVFKLSLTDAAS. It acts as an inhibitor for wild type full length tau aggregation. | ISAD1 peptide with amino acid sequence of SVFKLSLTDAAS. It acts as an inhibitor for wild type full length tau aggregation. | ||
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===Dry Lab=== | ===Dry Lab=== | ||
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ISAD1 is modeled by AlphaFold2, Apptest, ITASSER, best model obtained from Apptest. | ISAD1 is modeled by AlphaFold2, Apptest, ITASSER, best model obtained from Apptest. | ||
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/isal1-qa.png" style="margin-left:75px;" alt="" width="800" /></p> | <p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/isal1-qa.png" style="margin-left:75px;" alt="" width="800" /></p> | ||
</html> | </html> | ||
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| + | <span class='h3bb'> <p style=" font-weight: bold; font-size:17px;"> Sequence and Features</p> </span> | ||
| + | <partinfo>BBa_K4165152 SequenceAndFeatures</partinfo> | ||
Revision as of 13:50, 6 October 2022
ISAD1 Peptide
Tau binding peptide targeting the PHF seed of Tau
Usage and Biology
ISAD1 peptide with amino acid sequence of SVFKLSLTDAAS. It acts as an inhibitor for wild type full length tau aggregation.
Dry Lab
Modeling
ISAD1 is modeled by AlphaFold2, Apptest, ITASSER, best model obtained from Apptest.
Figure 1.: Predicted 3D structure of Synthetic peptide ISAD1.
Table 1: Quality assessment parameters of ISAD1 model.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
1. Aillaud, I., Kaniyappan, S., Chandupatla, R. R., Ramirez, L. M., Alkhashrom, S., Eichler, J., ... & Funke, S. A. (2022). A novel D-amino acid peptide with therapeutic potential (ISAD1) inhibits aggregation of neurotoxic disease-relevant mutant Tau and prevents Tau toxicity in vitro. Alzheimer's research & therapy, 14(1), 1-19.