Enhanced self-assembly of the 7–12 sequence of amyloid-β peptide by tyrosine bromination

Daniele Maiolo, Andrea Pizzi, Alessandro Gori, Greta Bergamaschi, Claudia Pigliacelli, Lara Gazzera, Alessandra Consonni, Fulvio Baggi, Fabio Moda, Francesca Baldelli Bombelli, Pierangelo Metrangolo*, Giuseppe Resnati

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

2 Citations (Scopus)


Alzheimer’s disease (AD) is a serious neuropathology related to the misfolded assembly state of amyloid-beta (Aβ40 and Aβ42) peptides. It has been demonstrated that protein post-translation modifications (PPTMs) of the more hydrophilic N-term moiety of the Aβ peptide affect its aggregation kinetics and interaction with the environment. Considering that chlorination and bromination are non-canonical PPTMs found in various metabolic pathways and often correlated to inflammatory responses, halogenation of the Y10 of the Aβ N-term could be a putative in vivo modification with implications in the Aβ peptide aggregation propensity. In this framework, we chose as a model system, a short peptide sequence, DSGYEV (i.e. residues 7–12 of the Aβ N-term) and studied its self-assembly behaviour in comparison to its chlorinated and brominated derivatives. Our results show that Y10 halogenation works as a molecular trigger of the peptide self-assembly in solution, promoting the formation of more structured aggregates.

Original languageEnglish
JournalSupramolecular Chemistry
Publication statusE-pub ahead of print - 1 Jan 2020
MoE publication typeA1 Journal article-refereed


  • bromine
  • Halogen bonding
  • halogenation
  • peptide
  • supramolecular chemistry

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