Difference between revisions of "Part:BBa K4165153"
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===Usage and Biology===
 
===Usage and Biology===
  
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WMW is a peptide with amino acid sequence of DVWMWNKKRK, 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. WMW can bind to PHF* in a mean that can disrupt the interface between each PHF* and consequently reduce the aggregates.
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WMW is a peptide with amino acid sequence of DVWMWNKKRK, 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 deriveS tau aggregation. WMW can bind to PHF* in a way that can disrupt the interface between each PHF* and consequently reduce the aggregates.
  
 
<span class='h3bb'> <p style=" font-weight: bold; font-size:17px;"> Sequence and Features</p> </span>
 
<span class='h3bb'> <p style=" font-weight: bold; font-size:17px;"> Sequence and Features</p> </span>

Revision as of 17:20, 10 October 2022


WMW

Tau binding peptide targeting the PHF* seed of Tau

Usage and Biology

WMW is a peptide with amino acid sequence of DVWMWNKKRK, 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 deriveS tau aggregation. WMW can bind to PHF* in a way that can disrupt the interface between each PHF* and consequently reduce the aggregates.

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

WMW is modeled by Apptest and TrRosetta, best model obtained from TrRosetta. 


                            Figure 1.: Predicted 3D structure of Synthetic peptide WMW.


Table 1: Quality assessment parameters of WMW 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.