1.
ChemistryOpen
; 9(2): 253-260, 2020 02.
Artículo
en Inglés
| MEDLINE
| ID: mdl-32110506
RESUMEN
Here, we demonstrate that introduction of halogen atoms at the tyrosine 10â phenol ring of the DSGYEV sequence derived from the flexible amyloid-ß 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.