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Enhanced self-assembly of the 7–12 sequence of amyloid-β peptide by tyrosine bromination
Supramolecular Chemistry  (IF1.688),  Pub Date : 2020-03-01, DOI: 10.1080/10610278.2020.1734203
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

ABSTRACT 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. Graphical abstract