Cell-Surface Glycan Labeling and Sensing

Abstract

Cell-surface glycans are abundant and complex and play a critical role in maintaining protein stability, regulating cell behavior, and participating in cell communication. Obtaining structural information on glycans in situ is helpful to further understand the role of glycans in the physiological and pathological processes of cells and the regulatory mechanism. To achieve this, we can use recognition or labeling strategies to convert the presence of glycans on the cell surface into signals that can be detected. Currently, many different types of in situ sensing strategies for glycans have been developed. The spatial control of the conversion process can realize the restriction of glycan detection to specific proteins, and the introduction of signal amplification technology into the conversion process can improve the sensitivity of sensing. In this paper, the recent progress of glycan labeling methods and sensing technology is reviewed, and the future development direction is prospected.

Functional Interface for Glycoprotein Sensing: Focusing on Biosensors

“…Another more promising future development should be directed to the precise discrimination of specific different glycoforms on glycoproteins and the in situ cell surface glycan sensing, labeling or imaging, which have been attracting much research interests. ,, Glycans on the cell surface would change with the progress of diseases, and aberrant glycosylation is often related to tumor development, so intricate glycosylation patterns are gradually becoming new biomarkers for early diagnosis of various diseases.…”

“…Another more promising future development should be directed to the precise discrimination of specific different glycoforms on glycoproteins and the in situ cell surface glycan sensing, labeling or imaging, which have been attracting much research interests. 41,74,75 (…”

“…However, lectins are able to exist in oligomer structures with multiple binding sites to simultaneously interact with different glycans of the same glycoprotein or with different arms of a branched oligosaccharide, thus achieving multivalent interaction to boost selectivity and affinity. 41 Lectins have been utilized as capable recognition element to enable glycoprotein identification, profiling and sensing. 42−45 Tkac and co-workers have developed a series of lectin-based impedimetric biosensors for the sensitive detection and glycoprofiling of glycoproteins.…”

“…Owing to the relatively shallow binding pocket on the lectin, the affinity of lectin-glycan is usually in the μM range. However, lectins are able to exist in oligomer structures with multiple binding sites to simultaneously interact with different glycans of the same glycoprotein or with different arms of a branched oligosaccharide, thus achieving multivalent interaction to boost selectivity and affinity . Lectins have been utilized as capable recognition element to enable glycoprotein identification, profiling and sensing. − Tkac and co-workers have developed a series of lectin-based impedimetric biosensors for the sensitive detection and glycoprofiling of glycoproteins. , Recently, Qu and co-worker reported to modify lectin of concanavalin A (Con A) on metal–organic framework material of MIL-101­(Cr)-NH 2 to afford an electrochemical impedimetric biosensing platform of Con A@MIL-101­(Cr)-NH 2 for glycoprotein detection …”