Difference between revisions of "Part:BBa K4165144"
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===Usage and Biology=== | ===Usage and Biology=== | ||
− | MINK is a peptide with amino acid sequence of DVQMINKKRK, it is designed to inhibit the fibrillization 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. MINK can bind to PHF* in a mean that can disrupt the interface between each PHF* and consequently reduce the aggregates. Its | + | MINK is a peptide with amino acid sequence of DVQMINKKRK, it is designed to inhibit the fibrillization 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. MINK 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 22.6 μM. |
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===Dry Lab=== | ===Dry Lab=== | ||
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+ | <span class='h3bb'> <p style=" font-weight: bold; font-size:17px;"> Sequence and Features</p> </span> | ||
+ | <partinfo>BBa_K4165144 SequenceAndFeatures</partinfo> | ||
===References=== | ===References=== |
Revision as of 13:44, 6 October 2022
MINK Peptide
Tau binding peptide targeting the PHF seed of Tau
Usage and Biology
MINK is a peptide with amino acid sequence of DVQMINKKRK, it is designed to inhibit the fibrillization 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. MINK 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 22.6 μM.
Dry Lab
Modeling
MINK is modeled by AlphaFold2, Apptest, ITAsser and TrRosetta, best model obtained from Apptest
Figure 1.: Predicted 3D structure of Synthetic peptide MINK.
Table 1: Quality assessment parameters of MINK 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.