An enrichment method based on synergistic and reversible covalent interactions for large-scale analysis of glycoproteins. Xiao, H., Chen, W., Smeekens, J. M., & Wu, R. Nature Communications, 9(1):1692, April, 2018. Number: 1 Publisher: Nature Publishing Group![An enrichment method based on synergistic and reversible covalent interactions for large-scale analysis of glycoproteins [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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.
@article{xiao_enrichment_2018,
title = {An enrichment method based on synergistic and reversible covalent interactions for large-scale analysis of glycoproteins},
volume = {9},
copyright = {2018 The Author(s)},
issn = {2041-1723},
url = {https://www.nature.com/articles/s41467-018-04081-3},
doi = {10.1038/s41467-018-04081-3},
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.},
language = {en},
number = {1},
urldate = {2023-03-07},
journal = {Nature Communications},
author = {Xiao, Haopeng and Chen, Weixuan and Smeekens, Johanna M. and Wu, Ronghu},
month = apr,
year = {2018},
note = {Number: 1
Publisher: Nature Publishing Group},
keywords = {Glycoproteins, Glycosylation, Protein enrichment, Proteomics},
pages = {1692},
}
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