Published May 12, 2022
| Version v1
Journal article
Open
Fast protein modification in the nanomolar concentration range using an oxalyl amide as latent thioester
Authors/Creators
-
1.
Institut Pasteur de Lille
- 2. Université de Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille
- 3. CNRS
- 4. Université de Lille, CNRS, Centrale Lille
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5.
BOKU University
-
6.
Austrian Centre of Industrial Biotechnology (Austria)
- 7. CNRS Délégation Nord Pas-de-Calais et Picardie
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8.
École Centrale de Lille
Description
Description of site-specific chemical protein ligation using oxoSEA chemistry. The article’s Supporting Information, containing the data that support the study’s findings, is included.
Abstract (English)
We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable reagents, they can be activated on demand to enable ligation reactions with peptide concentrations as low as a few hundred nM at rates approaching 30 M-1 s-1 .
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SnellaAngewChemIntEdEngl2022(61(29))e202204992.pdf
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