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Serine-Selective Bioconjugation
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DOI：10.1021/jacs.0c05595.png)
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Abstract
En 中文
This Communication reports the first general method for rapid, chemoselective, and modular functionalization of serine residues in native polypeptides, which uses a reagent platform based on the P(V) oxidation state. This redox-economical approach can be used to append nearly any kind of cargo onto serine, generating a stable, benign, and hydrophilic phosphorothioate linkage. The method tolerates all other known nucleophilic functional groups of naturally occurring proteinogenic amino acids. A variety of applications can be envisaged by this expansion of the toolbox of site-selective bioconjugation methods.
Keywords:
AB-INITIO
PROTEIN PHOSPHATASES
ACTIVE-SITE
HYDROLYSIS
UBIQUITIN
VANCOMYCIN
REDUCTION
MECHANISM
REAGENTS
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15.6
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