Glycoprotein analysis using lectin microcolumns and capillary electrophoresis: Characterization of alpha1-acid glycoprotein by combined separation methods

Zhang, Chenhua; Schumacher, Katherine N.; Dodds, Eric D.; Hage, David S.

doi:10.1016/j.jchromb.2021.122855

Cited by 5 publications

(3 citation statements)

References 38 publications

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“…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 …”

Section: Receptors For Glycoproteinsmentioning

confidence: 99%

Functional Interface for Glycoprotein Sensing: Focusing on Biosensors

Qu,

2024

Langmuir

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Glycosylated proteins or glycoproteins make up a large family of glycoconjugates, and they participate in a variety of fundamental biological events. Glycoproteins have become important biomarkers in the diagnosis and treatment of a number of tumors. Biosensors are quite suitable for glycoprotein detection. The design and fabrication of a functional sensing interface play a crucial role in the biosensor construction to target glycoproteins. The functional interface, particularly receptors, typically determines the key characteristics of a biosensor, such as selectivity and sensitivity. Antibody, peptide, aptamer, boronic acid derivative, lectin, and molecularly imprinted polymer are all capable receptors for glycoprotein recognition, and each of these will be discussed. Most glycoproteins exist in low abundance, thus rendering signal amplification techniques indispensable. Nucleic acid-mediated and nanomaterial-mediated signal amplification for the detection of glycoproteins will be focused on herein. This review aims to highlight these different functional interfaces for glycoprotein sensing.

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Section: Receptors For Glycoproteinsmentioning

confidence: 99%

Functional Interface for Glycoprotein Sensing: Focusing on Biosensors

Qu,

2024

Langmuir

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“…Traditional reversed phase liquid chromatography (RPLC) methods (C18, C4, PLRP, and others) are suitable for the separation of cleaved permethylated glycans, 32 small glycopeptides, [33][34][35] and some intact proteins, 21 but do not always provide sufficient resolution of larger glycans and glycosylated proteins. Capillary electrophoresis (CE), which involves the separation of analytes based on their electrophoretic mobilities, has shown some success in separating intact glycoproteins, 36,37 along with cleaved glycans. 38 Hydrophilic interaction chromatography (HILIC) has been widely adopted for the separation of cleaved glycans, 39 and glycopeptides, [40][41][42] and more recently has been adapted for intact glycoproteins.…”

Section: Introductionmentioning

confidence: 99%

Hydrophilic interaction chromatography coupled to ultraviolet photodissociation affords identification, localization, and relative quantitation of glycans on intact glycoproteins

James,

A.M. van der Zon,

Escobar

et al. 2024

Preprint

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Protein glycosylation is implicated in a wide array of diseases, yet glycoprotein analysis remains elusive owing to the extreme heterogeneity of glycans including microheterogeneity at the same amino acid residue (glycosite). Top-down mass spectrometry (MS) allows precise identification and localization of glycans on intact proteins, and coupling top-down MS with chromatography allows time-resolved characterization of glycoforms. Here, we couple ultraviolet photo-dissociation (UVPD) to hydrophilic interaction chromatography (HILIC) to advance the characterization of glycoproteins ranging from 15-34 kDa, offering site localization of glycans, providing sequence coverages up to 93% and relative quantitation of individual glycoforms.

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“…It is primarily secreted in the liver, but also in the heart or gastrointestinal tract [ 20 ]. α1AGP serves as an acute-phase protein, and its secretion is stimulated by inflammation or infection [ 21 , 22 ]. It exerts immunomodulatory properties and takes part in drug transport [ 23 ].…”

Section: Introductionmentioning

confidence: 99%

Tumor Necrosis Factor (TNF) α, Endothelin (ET) 1 and α1-Acid Glycoprotein (AGP) as Potential Urine and Serum Markers of Metabolic Complications in Psoriasis?

Nowowiejska

Baran

Hermanowicz

et al. 2023

Dermatol Ther (Heidelb)

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Introduction Psoriasis, one of the most frequent dermatoses, strongly associated with metabolic disorders which increase patients’ comorbidity and mortality. Hence, it is essential to look for markers of such complications. Our aim was to assess the clinical utility of urinary tumor necrosis factor alpha (TNFα), endothelin 1 (ET-1) and α1-acid glycoprotein (α1AGP) as well as their serum concentrations as markers of metabolic complications in psoriatics, and to examine the relations of these markers to clinical and demographic parameters. Methods The study involved 60 patients with plaque psoriasis and 30 volunteers without skin diseases (the control group). Serum and urinary concentrations of TNFα, ET-1 and α1AGP were measured by ELISA. Psoriasis severity was assessed using the psoriasis activity and severity index (PASI). Routine laboratory investigations were additionally performed. Results All serum markers were significantly higher in the patients compared to the controls. TNFα was undetectable in the urine in half of the patients. The urinary ET-1/creatinine concentration ratio was significantly lower in the psoriatics than the controls, whereas the absolute urinary α1AGP was significantly higher and the α1AGP/creatinine ratio was insignificantly different. There was no correlation between serum or urinary markers and PASI. All serum markers were higher in patients with psoriasis lasting less than 15 years. Conclusions Serum TNFα, ET-1 and α1AGP seem to be useful biomarkers of metabolic syndrome in psoriatics. ET-1 could perhaps become a urinary marker of metabolic disorders in psoriatics, but further studies are required to confirm that a decreased ET-1 concentration in urine is a reliable predictive tool. Increased urinary α1AGP also requires more in-depth research as a potential marker. TNFα urine assessment does not seem to be useful for screening for metabolic disorders in psoriatics. Serum or urinary TNFα, ET-1 and α1AGP do not seem to be associated with psoriasis severity or duration.

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Glycoprotein analysis using lectin microcolumns and capillary electrophoresis: Characterization of alpha1-acid glycoprotein by combined separation methods

Cited by 5 publications

References 38 publications

Functional Interface for Glycoprotein Sensing: Focusing on Biosensors

Functional Interface for Glycoprotein Sensing: Focusing on Biosensors

Hydrophilic interaction chromatography coupled to ultraviolet photodissociation affords identification, localization, and relative quantitation of glycans on intact glycoproteins

Tumor Necrosis Factor (TNF) α, Endothelin (ET) 1 and α1-Acid Glycoprotein (AGP) as Potential Urine and Serum Markers of Metabolic Complications in Psoriasis?

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