Halogenation of the N ‐Terminus Tyrosine 10 Promotes Supramolecular Stabilization of the Amyloid‐β Sequence 7–12 - Université de Lorraine Access content directly
Journal Articles ChemistryOpen Year : 2020

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

Abstract

This paper is dedicated to Prof. Jean-Marie Lehn on his 80th birth anniversary. 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.
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Dates and versions

hal-02492476 , version 1 (27-05-2020)

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Daniele Maiolo, Andrea Pizzi, Alessandro Gori, Lara Gazzera, Nicola Demitri, et al.. Halogenation of the N ‐Terminus Tyrosine 10 Promotes Supramolecular Stabilization of the Amyloid‐β Sequence 7–12. ChemistryOpen, 2020, 9 (2), pp.253-260. ⟨10.1002/open.201900350⟩. ⟨hal-02492476⟩
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