Difference between revisions of "Part:BBa K4165144"

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<partinfo>BBa_K4165144 short</partinfo>
 
<partinfo>BBa_K4165144 short</partinfo>
  
Tau binding peptide targeting the PHF seed of Tau
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A synthetic peptide that is used for targeting misfolded tau protein (BBa_K4165009) as it binds to PHF6 of tau fibrils.
  
 
===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 IC50 for inhibition of tau aggregates were 22.6 μM.  
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MINK is a peptide with amino acid sequence of DVQMINKKRK, it is acquired by mirror phage display to inhibit the fibrillization of tau which is one of the main drivers of Alzheimer’s disease and other dementia types. PHF* (VQIINK) is one of the sites that derives tau aggregation. MINK can bind to PHF* in a way that can disrupt the interaction between the fibrils and consequently reduce the aggregates. Its IC<sub>50</sub> for inhibition of tau aggregates were 22.6 μM.  
  
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<span class='h3bb'> <p style=" font-weight: bold; font-size:17px;"> Sequence and Features</p> </span>
<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K4165144 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K4165144 SequenceAndFeatures</partinfo>
  
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<p style=" font-weight: bold; font-size:14px;"> Modeling </p>
 
<p style=" font-weight: bold; font-size:14px;"> Modeling </p>
MINK is modeled by AlphaFold2, Apptest, ITAsser and TrRosetta, best model obtained from Apptest
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MINK was modeled by AlphaFold2, Apptest, ITAsser and TrRosetta, and the best model obtained from Apptest ranking 6 out of 6
 
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/mink.png" style="margin-left:200px;" alt="" width="300" /></p>
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/mink.png" style="margin-left:300px;" alt="" width="300" /></p>
 
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/mink-qa.png" style="margin-left:75px;" alt="" width="800" /></p>
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<p><img src="https://static.igem.wiki/teams/4165/wiki/parts-registry/mink-qa.png" style="margin-left:50px;" alt="" width="800" /></p>
 
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===References===
 
===References===
1. Reference
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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.
  
  

Latest revision as of 13:37, 11 October 2022


MINK Peptide

A synthetic peptide that is used for targeting misfolded tau protein (BBa_K4165009) as it binds to PHF6 of tau fibrils.

Usage and Biology

MINK is a peptide with amino acid sequence of DVQMINKKRK, it is acquired by mirror phage display to inhibit the fibrillization of tau which is one of the main drivers of Alzheimer’s disease and other dementia types. PHF* (VQIINK) is one of the sites that derives tau aggregation. MINK can bind to PHF* in a way that can disrupt the interaction between the fibrils and consequently reduce the aggregates. Its IC50 for inhibition of tau aggregates were 22.6 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

MINK was modeled by AlphaFold2, Apptest, ITAsser and TrRosetta, and the best model obtained from Apptest ranking 6 out of 6


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


Table 1: Quality assessment parameters of MINK 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.