chromatography, monolith, glycan, glycoprotein, lectin, mass spectrometry
There is continuous effort towards developing monolithic materials as solid supports for the separation, enrichment, and digestion of glycoproteins. The intention of this review is to discuss and summarize work reported in this area during the period 2015–2021 as a follow-up to our prior review. Reports from the past three decades have already proven the advantages of monolithic materials, such as the ease with which they can be prepared and functionalized, their high permeability and low resistance to mass transfer, and their stability over a wide range of pH. Recent works on glycoprotein analysis introduce different strategies in using monolithic materials specifically in separation, enrichment, and identification of glycoproteins, glycopeptides, and free glycans. A majority of these are focused on boronic acid affinity-based technique and others on lectin affinity and HILIC-based techniques. There are also newly developed ligands that utilize different interactions with glycans, such as encapsulation into β-cyclodextrin vesicles, CH- or OH-π interactions with fullerenes, immunoaffinity with monoclonal antibodies, H-bonding interactions with metallophthalocyanines, coordination interactions with cobalt phthalocyanine tetracarboxylic acid, and hydrophilic interaction with cyclodextrin molecular tubes, zwitterionic iminodiacetic acid, and boric acid. Recent strategies for developing on-line, multidimensional systems use immobilized monolithic enzyme reactors (IMERs) for high-throughput glycoprotein analysis. These works serve as contributions to better understand glycan structure-function relationship, as glycoproteins are now widely accepted disease biomarkers.
Alla, Allan and Stine, Keith, "Recent Strategies for Using Monolithic Materials in Glycoprotein and Glycopeptide Analysis" (2022). Chemistry & Biochemistry Faculty Works. 77.
Available at: https://irl.umsl.edu/chemistry-faculty/77