Difference between revisions of "Part:BBa K4165006"
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A short synthetic peptide acquired by mirror image phage display for binding to tau fibrils at its seed sequence ‘VQIVYK’ called the PHF6. The aggregation of microtubule-associated tau protein starts at this seed to form neurofibrillary tangles inside the brain, which are the main cause of Alzheimer’s disease (AD). Accordingly, this peptide would be suitable to act as our targeting domain for the aggregations. | A short synthetic peptide acquired by mirror image phage display for binding to tau fibrils at its seed sequence ‘VQIVYK’ called the PHF6. The aggregation of microtubule-associated tau protein starts at this seed to form neurofibrillary tangles inside the brain, which are the main cause of Alzheimer’s disease (AD). Accordingly, this peptide would be suitable to act as our targeting domain for the aggregations. | ||
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| + | ===Dry Lab characterization=== | ||
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===References=== | ===References=== | ||
Revision as of 18:13, 4 October 2022
TD28rev (Tau binding peptide)
A synthetic peptide that is used for targeting misfolded tau protein (BBa_K4165009) as it binds to PHF6 of tau fibrils.
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Usage and Biology
A short synthetic peptide acquired by mirror image phage display for binding to tau fibrils at its seed sequence ‘VQIVYK’ called the PHF6. The aggregation of microtubule-associated tau protein starts at this seed to form neurofibrillary tangles inside the brain, which are the main cause of Alzheimer’s disease (AD). Accordingly, this peptide would be suitable to act as our targeting domain for the aggregations.
Dry Lab characterization
References
Dammers, C., Yolcu, D., Kukuk, L., Willbold, D., Pickhardt, M., Mandelkow, E., ... & Funke, S. A. (2016). Selection and Characterization of Tau Binding ᴅ-Enantiomeric Peptides with Potential for Therapy of Alzheimer Disease. PLoS One, 11(12), e0167432.