101. Enrichment of IgG and HRP glycoprotein by dipeptide-based polymeric material
- Author
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Xintong Zheng, Fusheng Zhang, Yanyan Zhao, Yuting Xiong, Xiaoyu Zhang, Zhenqiang Shi, Shengxu Qian, Haijuan Qin, and Guangyan Qing
- Subjects
Immunoglobulin G ,Glycopeptides ,Dipeptides ,Silicon Dioxide ,Horseradish Peroxidase ,Analytical Chemistry ,Glycoproteins - Abstract
Separation, purification, and identification of glycoproteins are essential for understanding their vital roles in biological and pathological processes. However, glycoproteins are difficult to be captured due to their low abundance, strong interference from non-glycosylated proteins. Here, we report a promising dipeptide-based saccharide recognition platform to selectively enrich two typical glycoproteins, named immunoglobin G (IgG) and horseradish peroxidase (HRP). Different from the conventional glycoprotein enrichment method based on boronic acid affinity or hydrophilic interaction with glycans, the present method was established based on affinity between Pro-Glu (PE) dipeptide and mannose, which is a key unit in the pentasaccharide core of the IgG and HRP glycans. The prepared PE homopolymer surface was proved to selectively bind IgG and HRP superior to that of bovine serum albumin (BSA). Benefiting from this feature, selective enrichment of IgG and HRP was achieved from a protein mixture containing 200-fold BSA interference by using polyPE@SiO
- Published
- 2021