Halogenation of the N-Terminus Tyrosine 10 Promotes Supramolecular Stabilization of the Amyloid-β Sequence 7–12

Daniele Maiolo, Andrea Pizzi, Alessandro Gori, Lara Gazzera, Nicola Demitri, Alessandro Genoni, Fulvio Baggi, Fabio Moda, Giancarlo Terraneo, Francesca Baldelli Bombelli, Pierangelo Metrangolo, Giuseppe Resnati

Research output: Contribution to journalArticlepeer-review

Abstract

Here, we demonstrate that introduction of halogen atoms at the tyrosine 10 phenol ring of the DSGYEV sequence derived from the flexible amyloid-β N-terminus, promotes its self-assembly in the solid state. In particular, we report the crystal structures of two halogen-modified sequences, which we found to be stabilized in the solid state by halogen-mediated interactions. The structural study is corroborated by Non-Covalent Interaction (NCI) analysis. Our results prove that selective halogenation of an amino acid enhances the supramolecular organization of otherwise unstructured biologically-relevant sequences. This method may develop as a general strategy for stabilizing highly polymorphic peptide regions.

Original languageEnglish
Pages (from-to)253-260
Number of pages8
JournalChemistryOpen
Volume9
Issue number2
DOIs
Publication statusPublished - Feb 1 2020

Keywords

  • bromine
  • crystal engineering
  • halogen bonding
  • peptide
  • supramolecular

ASJC Scopus subject areas

  • Chemistry(all)

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