Fast Protein Modification in the Nanomolar Concentration Range Using an Oxalyl Amide As Latent Thioester
Overview
Authors
Affiliations
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 s .
Incorporation of a Highly Reactive Oxalyl Thioester-Based Interacting Handle into Proteins.
Grain B, Desmet R, Snella B, Melnyk O, Agouridas V Org Lett. 2023; 25(27):5117-5122.
PMID: 37384828 PMC: 10353032. DOI: 10.1021/acs.orglett.3c01846.
Ollivier N, Senechal M, Desmet R, Snella B, Agouridas V, Melnyk O Nat Commun. 2022; 13(1):6667.
PMID: 36335111 PMC: 9637170. DOI: 10.1038/s41467-022-34392-5.
Redox-Controlled Chemical Protein Synthesis: Sundry Shades of Latency.
Agouridas V, Ollivier N, Vicogne J, Diemer V, Melnyk O Acc Chem Res. 2022; 55(18):2685-2697.
PMID: 36083810 PMC: 9494750. DOI: 10.1021/acs.accounts.2c00436.