Protocol for protein modification using oxalyl thioester-mediated chemoselective ligation
Authors/Creators
- Terzani, Francesco (Researcher)1
- Wang, Chen (Researcher)1
- Rostami, Simindokht (Researcher)2
- Desmet, Rémi (Researcher)1
- Snella, Benoît (Researcher)1
- Sénéchal, Magalie (Researcher)1
-
Wiltschi, Birgit
(Researcher)2, 3
- Vicogne, Jérôme (Researcher)1
-
Melnyk, Oleg
(Researcher)4
-
Agouridas, Vangelis
(Researcher)1, 5
- 1. Université de Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille
-
2.
BOKU University
-
3.
Austrian Centre of Industrial Biotechnology (Austria)
- 4. CNRS Délégation Nord Pas-de-Calais et Picardie
- 5. École Centrale de Lille
Description
Protocol for the site-specific modification of proteins and peptides using fast oxoSEA ligation chemistry. The article’s Supporting Information, containing the data that support the study’s findings, is included.
Abstract (English)
The development of fast ligation chemistries for the site-specific modification of proteins has become a major focus in chemical biology. We describe steps for preparing an oxalyl thioester precursor in the form of an N-oxalyl perhydro-1,2,5-dithiazepine handle, i.e., the oxoSEA group, and incorporating it into a peptide modifier using solid phase peptide synthesis. We then detail procedures for its application for the modification of an N-terminal Cys-containing B1 domain of the streptococcal G protein using the native chemical ligation. For complete details on the use and execution of this protocol, please refer to Snella, et al. (2022) Angew Chem Int Ed Engl 61(29): e202204992 (doi: 10.1002/anie.202204992).
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TerzaniSTARProtoc2024(5(4))103390.pdf
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