ArticleBrain communications2025
Dehydroamino acids and their crosslinks in Alzheimer's disease aggregates.
Article in Brain communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Cyanamide-Induced Desulfhydration Enables Access to α,β-Dehydropeptides.Organic letters · 2026Article
- Metal Oxides Catalyze Formation of Dehydroamino Acids by Phosphate β-Elimination Under Physiological Conditions.Angewandte Chemie (International ed. in English) · 2026Article
- Protein-Protein Cross-Linking by a DNA Damage-Derived Histone Modification.Journal of the American Chemical Society · 2026Article
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Authors and funding
5 authors.
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Abstract
Alzheimer's disease (AD) is characterized by the accumulation of protein aggregates, which are thought to be influenced by posttranslational modifications (PTMs). Dehydroamino acids (DHAAs) are rarely observed PTMs that contain an electrophilic alkene capable of forming protein-protein crosslinks, which may lead to protein aggregation. We report here the discovery of DHAAs in the protein aggregates from AD, constituting an unknown and previously unsuspected source of extensive proteomic complexity. We used mass spectrometry-based proteomics to discover 404 sites of DHAA formation in 171 proteins from protein aggregate-enriched human brain samples, 6-fold more sites than observed in the soluble protein fractions. The DHAA modifications are observed both directly and in the form of conjugates after reacting with abundant cellular nucleophiles or crosslinking to nucleophilic amino acid residues. We report 11 such crosslinks, including three in the Tau protein, which are 10-fold more abundant in AD samples compared with age-matched controls. Many of the proteins found to contain DHAAs and their conjugates are involved in protein aggregation or pathways dysregulated in AD. DHAAs are prevalent modifications in the AD brain proteome and give rise to protein crosslinks that may contribute to protein aggregation.
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