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

Research output: Contribution to journalArticleScientificpeer-review


  • 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

Research units

  • Polytechnic University of Milan
  • CNR-ENEA-EURATOM Association
  • IRCCS Fondazione Istituto Neurologico Carlo Besta - Milano


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

    Research areas

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

ID: 41730828