Light-Controlled Tyrosine Nitration of Proteins.
Angew Chem Int Ed Engl
; 60(24): 13414-13422, 2021 06 07.
Article
en En
| MEDLINE
| ID: mdl-33847040
ABSTRACT
Tyrosine nitration of proteins is one of the most important oxidative post-translational modifications in vivo. A major obstacle for its biochemical and physiological studies is the lack of efficient and chemoselective protein tyrosine nitration reagents. Herein, we report a generalizable strategy for light-controlled protein tyrosine nitration by employing biocompatible dinitroimidazole reagents. Upon 390â
nm irradiation, dinitroimidazoles efficiently convert tyrosine residues into 3-nitrotyrosine residues in peptides and proteins with fast kinetics and high chemoselectivity under neutral aqueous buffer conditions. The incorporation of 3-nitrotyrosine residues enhances the thermostability of lasso peptide natural products and endows murine tumor necrosis factor-α with strong immunogenicity to break self-tolerance. The light-controlled time resolution of this method allows the investigation of the impact of tyrosine nitration on the self-assembly behavior of α-synuclein.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Tirosina
/
Factor de Necrosis Tumoral alfa
/
Alfa-Sinucleína
/
Luz
/
Nitratos
Límite:
Animals
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Año:
2021
Tipo del documento:
Article
País de afiliación:
China