ArticleACS chemical neuroscience2025
Aberrant S293 Phosphorylation Drives Oligomerization of Tau Repeat R2: Insights from Molecular Dynamics Simulations.
Article in ACS chemical neuroscience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Aberrant phosphorylation, which is absent in healthy brains but present exclusively in the brains of individuals with Alzheimer's disease (AD), plays a critical role in AD development. It causes the dissociation of tau protein from microtubules, followed by the aggregation of tau protein into brain-toxic oligomers and fibrils. In our previous study, we investigated the impact of abnormal phosphorylation at S289 (pS289) on the oligomerization of tau repeat R2 peptides. In this work, we continue to investigate the effect of aberrant phosphorylation at residue S293 (pS293) on the R2 peptides. Our result indicated that pS293 also promotes oligomerization, which is similar to pS289. Both the phosphorylation-enhanced intramolecular and intermolecular interactions and β-sheet formation of phosphorylated R2 compared to that of the wild type. We observed that Na
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