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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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===References===
 
===References===

Revision as of 17:03, 10 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.

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:

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.

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.