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

© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA..

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.

Medienart:

E-Artikel

Erscheinungsjahr:

2020

Erschienen:

2020

Enthalten in:

Zur Gesamtaufnahme - volume:9

Enthalten in:

ChemistryOpen - 9(2020), 2 vom: 13. Feb., Seite 253-260

Sprache:

Englisch

Beteiligte Personen:

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

Links:

Volltext

Themen:

42HK56048U
Amino Acids
Amyloid beta-Peptides
Bromine
Crystal engineering
Halogen bonding
Journal Article
Peptide
Research Support, Non-U.S. Gov't
SBV4XY874G
Supramolecular
Tyrosine

Anmerkungen:

Date Completed 21.06.2021

Date Revised 21.06.2021

published: Electronic-eCollection

Citation Status MEDLINE

doi:

10.1002/open.201900350

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM307027295