Highly specific revelation of rat serum glycopeptidome by boronic acid-functionalized mesoporous silica

A high boronate avidity monolithic capillary for the selective enrichment of trace glycoproteins

“…Existing tools for the selective enrichment of glycoproteins mainly include lectins [4][5][6][7], antibodies [8,9], hydrazide [10][11][12][13][14], and boronate affinity materials [15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34]. However, lectins and antibodies are associated with apparent disadvantages, such as difficult to prepare and poor stability.…”

Mass spectrometric analysis of products of metabolic glycan engineering with azido-modification of sialic acids

“…Lectins have been used as enrichment media, such as concanavalin A (Con A), which has strong affinity for high mannose type glycoforms, lower affinity for hybrid chains, and nearly no affinity for complex glycans [12,13]. Methods based on hydrazide chemistry have been reported, exploiting oxidized cis-diol interactions [14,15], and other protocols focus on the capture of glycans through boronic acid interactions [16] or aniline groups functionalized to magnetic nanoparticles [17,18]. Hydrophilic interaction liquid chromatography (HILIC) approaches have shown to be simple, fast, and efficient relative to reversed-phase approaches for glycopeptide enrichment [19][20][21][22].…”

Synthesis and evaluation of carboxymethyl chitosan for glycopeptide enrichment

“…Furthermore, methods based on hydrazide chemistry have been reported which exploit oxidized cis-diol interactions [11,12], while other protocols have focused on the capture of glycans through boronic acid interactions [13], aniline groups functionalized to magnetic nanoparticles [14], or aminooxy-functionalized magnetic nanoparticles [15]. These approaches not only add additional steps to the workflow, but furthermore may compromise and forfeit structural information of the glycopeptide due to the harsh oxidation conditions necessary for release.…”