Facile preparation of microporous organic polymers functionalized macroporous hydrophilic resin for selective enrichment of glycopeptides.

A macroporous adsorption resin (MAR) with ∼10 μm diameter was synthesized by seed-swelling polymerization and further modified with a layer of microporous organic polymers (MOP) by "one-pot" solvothermal reaction. The resulting MAR@MOP exhibited high specific surface area of 131.3 m/g, which was higher than that of pristine MAR (57.8 m/g). The contact angle also decreased from 58.8° (MAR) to 24° (MAR@MOP), indicating that the MOP was successfully grafted onto the surface of MAR. The chemical composition of MAR@MOP was confirmed by Fourier-transform infrared spectroscopy, C NMR and element analysis. The enrichment efficiency of MAR@MOP to glycopeptides was demonstrated by trapping N-linked glycopeptides from tryptic digests of human immunoglobulin G (IgG), horseradish peroxidase (HRP) and bovine fetuin. Furthermore, 879 unique N-glycosylation sites in 811 unique glycopeptides sequence mapped to 516 N-glycosylated proteins were identified in three replicate analyses of proteins extracted from mouse liver. Therefore, this hydrophilic MOP-coated adsorbent would be applied in the enrichment and identification of low-abundance N-linked glycopeptides in complicated biological samples.