期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 61, 期 13, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202114154
关键词
Bioorthogonal Reaction; Cyanopyridylalanine; Genetic Encoding; Noncanonical Amino Acids; Protein Conjugation
资金
- Australian Research Council [FL170100019, DE190100015, DP200100348, DP210100088]
- Australian Research Council through a Centre of Excellence [CE200100012]
- Australian Research Council [DE190100015, FL170100019] Funding Source: Australian Research Council
Cyanopyridylalanines are non-canonical amino acids that can react with aminothiol compounds under physiological conditions in a biocompatible manner. Newly developed aminoacyl-tRNA synthetases enable the site-specific attachment of meta- and para-cyanopyridylalanine and the incorporation of a wide range of different functionalities. The outstanding utility of the cyanopyridine moiety is demonstrated by various applications in protein functionalization, in-cell macrocyclization, and protein stapling.
Cyanopyridylalanines are non-canonical amino acids that react with aminothiol compounds under physiological conditions in a biocompatible manner without requiring added catalyst. Here we present newly developed aminoacyl-tRNA synthetases for genetic encoding of meta- and para-cyanopyridylalanine to enable the site-specific attachment of a wide range of different functionalities. The outstanding utility of the cyanopyridine moiety is demonstrated by examples of i) post-translational functionalization of proteins, ii) in-cell macrocyclization of peptides and proteins, and iii) protein stapling. The biocompatible nature of the protein ligation chemistry enabled by the cyanopyridylalanine amino acid opens a new path to specific in vivo protein modifications in complex biological environments.
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