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Identification of potential sialic acid binding proteins on cell membrane by proximity chemical labeling

Abstract

The cell membrane contains a highly interactive glycan surface on a scaffold of proteins and lipids. Sialic acids are negatively charged monosaccharides, and the proteins that bind to sialic acids play important role in maintaining the integrity and collective functions of this interactive space. Sialic acid binding proteins are not readily identified and have nearly all been discovered empirically. In this research, we developed a proximity labeling method to characterize the proteins with oxidation by localized radicals produced in situ. The sites of oxidation were identified and quantified using a standard proteomic workflow. In this method, a clickable probe was synthesized and attached to modified sialic acids on the cell membrane, which functioned as a catalyst for the localized formation of radicals from hydrogen peroxide. The proteins in the sialic acid environment were labeled through amino acid oxidation, and were categorized into three groups including sialylated proteins, non-sialylated proteins with transmembrane domains, and proteins that are associated with the membrane with neither sialylated nor transmembrane domains. The analysis of these latter proteins showed that they were associated with binding functions including carbohydrate binding, anionic binding, and cationic binding, thereby revealing the nature of the sialic acid-protein interaction. This new tool identified potential sialic acid-binding proteins in the extracellular space and proteins that were organized around sialylated glycans in cells.

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Supplementary files

Publication details

The article was received on 20 Mar 2019, accepted on 14 May 2019 and first published on 14 May 2019


Article type: Edge Article
DOI: 10.1039/C9SC01360A
Chem. Sci., 2019, Accepted Manuscript
  • Open access: Creative Commons BY-NC license
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    Identification of potential sialic acid binding proteins on cell membrane by proximity chemical labeling

    Q. Li, Y. Xie, G. Xu and C. B. Lebrilla, Chem. Sci., 2019, Accepted Manuscript , DOI: 10.1039/C9SC01360A

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