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