TY - JOUR
T1 - Enhanced self-assembly of the 7–12 sequence of amyloid-β peptide by tyrosine bromination
AU - Maiolo, Daniele
AU - Pizzi, Andrea
AU - Gori, Alessandro
AU - Bergamaschi, Greta
AU - Pigliacelli, Claudia
AU - Gazzera, Lara
AU - Consonni, Alessandra
AU - Baggi, Fulvio
AU - Moda, Fabio
AU - Baldelli Bombelli, Francesca
AU - Metrangolo, Pierangelo
AU - Resnati, Giuseppe
N1 - Funding Information:
The authors are thankful to Fondazione Cariplo for funding the project PHAEDRA, no. 2014-0746. They also acknowledge the provision of facilities and technical support by Aalto University at OtaNano - Nanomicroscopy Center (Aalto-NMC).
Funding Information:
This work was supported by the Fondazione Cariplo [Project PHAEDRA, no. 2014-0746]. The authors are thankful to Fondazione Cariplo for funding the project PHAEDRA, no. 2014-0746. They also acknowledge the provision of facilities and technical support by Aalto University at OtaNano - Nanomicroscopy Center (Aalto-NMC).
Publisher Copyright:
© 2020, © 2020 Informa UK Limited, trading as Taylor & Francis Group.
Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 2020/4/2
Y1 - 2020/4/2
N2 - 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.
AB - 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.
KW - bromine
KW - Halogen bonding
KW - halogenation
KW - peptide
KW - supramolecular chemistry
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U2 - 10.1080/10610278.2020.1734203
DO - 10.1080/10610278.2020.1734203
M3 - Article
AN - SCOPUS:85079876240
VL - 32
SP - 247
EP - 255
JO - Supramolecular Chemistry
JF - Supramolecular Chemistry
SN - 1061-0278
IS - 4
ER -