2. Academic Validation
  3. Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan Labeling

Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan Labeling

  • Angew Chem Int Ed Engl. 2018 Feb 12;57(7):1817-1820. doi: 10.1002/anie.201711710.
Wei Qin 1,  Ke Qin 1,  Xinqi Fan 1,  Linghang Peng 1,  Weiyao Hong 1,  Yuntao Zhu 1,  Pinou Lv 1,  Yifei Du 1,  Rongbing Huang 1,  Mengting Han 1,  Bo Cheng 1,  Yuan Liu 1,  Wen Zhou 1,  Chu Wang 1,  Xing Chen 1
Affiliations

Affiliation

  • 1 College of Chemistry and Molecular Engineering, Peking-Tsinghua Center for Life Science, Beijing National Laboratory for Molecular Sciences, Synthetic and Functional Biomolecules Center, and Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, Peking University, Beijing, 100871, China.
PMID: 29237092 DOI: 10.1002/anie.201711710
Abstract

The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated Monosaccharides is described. This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades. It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).

Keywords

O-GlcNAc; S-glycosylation; chemoproteomics; labeling; unnatural monosaccharides.

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