Difference between revisions of "Part:BBa K4165151"
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M4W39 is a peptide with amino acid sequence of DVWMINKKWK, 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. M4W39 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 2.9 μM. | M4W39 is a peptide with amino acid sequence of DVWMINKKWK, 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. M4W39 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 2.9 μM. | ||
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| + | <span class='h3bb'> <p style=" font-weight: bold; font-size:17px;"> Sequence and Features</p> </span> | ||
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Revision as of 13:49, 6 October 2022
M4W39 Peptide
Tau binding peptide targeting the PHF seed of Tau
Usage and Biology
M4W39 is a peptide with amino acid sequence of DVWMINKKWK, 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. M4W39 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 2.9 μM.
Dry Lab
Modeling
modeled by AlphaFold2, Apptest, ITASSER, best model obtained from AlphaFold2
Figure 1.: Predicted 3D structure of Synthetic peptide M4W39.
Table 1: Quality assessment parameters of M4W39 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.