Published August 1, 2023
| Version v1
Journal article
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Anti-tau antibodies targeting a conformation-dependent epitope selectively bind seeds
Creators
- 1. Center for Alzheimers and Neurodegenerative Diseases and Department of Neurology, University of Texas Southwestern Medical Center
- 2. Center for Alzheimers and Neurodegenerative Diseases, University of Texas Southwestern Medical Center
- 3. Department of Pathology, University of Texas Southwestern Medical Center
Description
Tau protein undergoes conformational change to self-assemble and trigger neurodegeneration. We have proposed local unfolding events centered on P301 cis/trans isomerization, which expose amyloidogenic sequences. We used a non-natural peptide with a trans-proline to generate monoclonal antibodies that distinguish tau seeds from native tau in human brain. In addition to being important therapeutic and diagnostic leads, the activity of these antibodies supports structural studies implicating local conformational change in tau that underlies disease initiation.
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