Difference between revisions of "Part:BBa K4165146"
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WINK is a peptide with amino acid sequence of DVQWINKKRK, it is designed to inhibit the fibrilization of tau which is one of the main drivers of Alzheimer’s disease and other dementia diseases. PHF* (VQIINK) is the site that derive tau aggregation. WINK can bind to PHF* in a mean that can disrupt the interface between each PHF* and consequently reduce the aggregates. Its IC<sub>50</sub> for inhibition of tau aggregates were 28.9 μM. | WINK is a peptide with amino acid sequence of DVQWINKKRK, it is designed to inhibit the fibrilization of tau which is one of the main drivers of Alzheimer’s disease and other dementia diseases. PHF* (VQIINK) is the site that derive tau aggregation. WINK can bind to PHF* in a mean that can disrupt the interface between each PHF* and consequently reduce the aggregates. Its IC<sub>50</sub> for inhibition of tau aggregates were 28.9 μM. | ||
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<p style=" font-weight: bold; font-size:17px;"> Dry Lab: </p> | <p style=" font-weight: bold; font-size:17px;"> Dry Lab: </p> | ||
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===References=== | ===References=== | ||
Revision as of 13:46, 6 October 2022
WINK Peptide
Tau binding peptide targeting the PHF* seed of Tau
Usage and Biology
WINK is a peptide with amino acid sequence of DVQWINKKRK, it is designed to inhibit the fibrilization of tau which is one of the main drivers of Alzheimer’s disease and other dementia diseases. PHF* (VQIINK) is the site that derive tau aggregation. WINK can bind to PHF* in a mean that can disrupt the interface between each PHF* and consequently reduce the aggregates. Its IC50 for inhibition of tau aggregates were 28.9 μM.
Dry Lab:
Modeling:
WINK is modeled by AlphaFold2, Apptest, ITASSER, and TrRosetta, best model obtained from ITASSER.
Figure 1.: Predicted 3D structure of Synthetic peptide WINK.
Table 1: Quality assessment parameters of WINK model.
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]
References
1. Seidler, P. M., Boyer, D. R., Rodriguez, J. A., Sawaya, M. R., Cascio, D., Murray, K., ... & Eisenberg, D. S. (2018). Structure-based inhibitors of tau aggregation. Nature chemistry, 10(2), 170-176.