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T232K/K238Q Aerolysin Nanopore for Mapping Adjacent Phosphorylation Sites of a Single Tau Peptide.
- Source :
-
Small Methods . 11/13/2020, Vol. 4 Issue 11, p1-6. 6p. - Publication Year :
- 2020
-
Abstract
- Tau phosphorylation shows direct clinical importance as the hyperphosphorylation and aggregation of tau exists in a range of tauopathies. However, it is still challenging to study tau phosphorylation owing to its multiple and adjacent phosphorylation sites in the tau sequence. To address this challenge, here, a designed T232K/K238Q mutant aerolysin nanopore is introduced which synergistically incorporates the enhanced electrostatic interaction at T232K site and the high repelling barrier at K238Q site. The distinct current blockages produced by a T232K/K238Q aerolysin sensor achieve nearly 100% identification accuracy for the characteristic distribution of unphosphorylated tau peptide, pS262‐, pT263‐tau peptide, and pS262/pT263‐tau peptide. The excellent sensing ability of the T232K/K238Q nanopore originates from the extremely slow translocation speed which prolongs the duration up to tens or hundreds milliseconds for a nine‐amino‐acid peptide. It is envisioned that the design ideas of the T232K/K238Q aerolysin nanopore can be further applied to analyze other protein/peptide post‐translational modification as it provides the exquisite sensitivity for identifying the modification of single amino acids. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 23669608
- Volume :
- 4
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- Small Methods
- Publication Type :
- Academic Journal
- Accession number :
- 146975025
- Full Text :
- https://doi.org/10.1002/smtd.202000014