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Non-enzymatic protein templates amide bond formation and provides catalytic turnover

Authors :
Nicolas Brauckhoff
Laura Fang
Anissa Haim
Tom N. Grossmann
AIMMS
Organic Chemistry
Source :
Chemical Communications, 2023(5). Royal Society of Chemistry, Brauckhoff, N, Fang, L, Haim, A & Grossmann, T N 2023, ' Non-enzymatic protein templates amide bond formation and provides catalytic turnover ', Chemical Communications, vol. 2023, no. 5, pp. 5241–5244 . https://doi.org/10.1039/d3cc00514c
Publication Year :
2023

Abstract

The spatial alignment of functional groups is a central aspect of most catalytic processes. Protein scaffolds with their exceptional molecular recognition properties have evolved into powerful biological catalysts. However, the rational design of artificial enzymes starting from non-catalytic protein domains proved challenging. Herein, we report the use of a non-enzymatic protein as template for amide bond formation. Starting from a protein adaptor domain capable of simultaneously binding to two peptide ligands, we designed a catalytic transfer reaction based on the native chemical ligation. This system was used for the selective labelling of a target protein validating its high chemoselectivity and potential as a novel tool for the selective covalent modification of proteins.

Details

Language :
English
ISSN :
13597345
Volume :
2023
Issue :
5
Database :
OpenAIRE
Journal :
Chemical Communications
Accession number :
edsair.doi.dedup.....de97050086e4590b135cdc11c65269e4
Full Text :
https://doi.org/10.1039/d3cc00514c