Serine-Selective Bioconjugation

doi:10.1021/jacs.0c05595

Serine-Selective Bioconjugation

2020-09-23

64

OA

AI

J

Julien C. Vantourout

S

Srinivasa Rao Adusumalli

Gonçalo J. L. Bernardes *

P

Phil S. Baran *

DOI：10.1021/jacs.0c05595

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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.

Keyword:

AB-INITIO

PROTEIN PHOSPHATASES

ACTIVE-SITE

HYDROLYSIS

UBIQUITIN

VANCOMYCIN

REDUCTION

MECHANISM

REAGENTS

Serine-Selective Bioconjugation

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