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Nat Commun. 2018 Apr 27;9(1):1692. doi: 10.1038/s41467-018-04081-3.

An enrichment method based on synergistic and reversible covalent interactions for large-scale analysis of glycoproteins.

Xiao H1,2, Chen W1,2, Smeekens JM1,2, Wu R3,4.

Author information

1
School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
2
The Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
3
School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, 30332, USA. ronghu.wu@chemistry.gatech.edu.
4
The Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA, 30332, USA. ronghu.wu@chemistry.gatech.edu.

Abstract

Protein glycosylation is ubiquitous in biological systems and essential for cell survival. However, the heterogeneity of glycans and the low abundance of many glycoproteins complicate their global analysis. Chemical methods based on reversible covalent interactions between boronic acid and glycans have great potential to enrich glycopeptides, but the binding affinity is typically not strong enough to capture low-abundance species. Here, we develop a strategy using dendrimer-conjugated benzoboroxole to enhance the glycopeptide enrichment. We test the performance of several boronic acid derivatives, showing that benzoboroxole markedly increases glycopeptide coverage from human cell lysates. The enrichment is further improved by conjugating benzoboroxole to a dendrimer, which enables synergistic benzoboroxole-glycan interactions. This robust and simple method is highly effective for sensitive glycoproteomics analysis, especially capturing low-abundance glycopeptides. Importantly, the enriched glycopeptides remain intact, making the current method compatible with mass-spectrometry-based approaches to identify glycosylation sites and glycan structures.

PMID:
29703890
PMCID:
PMC5923262
DOI:
10.1038/s41467-018-04081-3
[Indexed for MEDLINE]
Free PMC Article

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