Difference between revisions of "Part:BBa K4165153"
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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. | 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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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/wmw-qa.png" style="margin-left:75px;" alt="" width="800" /></p> | <p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/wmw-qa.png" style="margin-left:75px;" alt="" width="800" /></p> | ||
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| + | <span class='h3bb'> <p style=" font-weight: bold; font-size:17px;"> Sequence and Features</p> </span> | ||
| + | <partinfo>BBa_K4165153 SequenceAndFeatures</partinfo> | ||
Revision as of 13:51, 6 October 2022
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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 derive tau aggregation. WMW can bind to PHF* in a mean that can disrupt the interface between each PHF* and consequently reduce the aggregates.
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.
Sequence and Features
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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.