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Halogenation of the N -Terminus Tyrosine 10 Promotes Supramolecular Stabilization of the Amyloid-β Sequence 7-12.
- Source :
-
ChemistryOpen [ChemistryOpen] 2020 Feb 25; Vol. 9 (2), pp. 253-260. Date of Electronic Publication: 2020 Feb 25 (Print Publication: 2020). - Publication Year :
- 2020
-
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.<br />Competing Interests: The authors declare no conflict of interest.<br /> (© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.)
Details
- Language :
- English
- ISSN :
- 2191-1363
- Volume :
- 9
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- ChemistryOpen
- Publication Type :
- Academic Journal
- Accession number :
- 32110506
- Full Text :
- https://doi.org/10.1002/open.201900350