Service Offered: High-Throughput Profiling of Protein N-Glycosylation Employing Linkage-Specific Sialic Acid Esterfication

Market sectors: Research, Biomarker Discovery, Glycosylation
Analysis, Patient stratification

The team of Professor Manfred Wuhrer at Leiden University Medical Center (LUMC), have developed a rapid, robust and linkage-specific high-throughput method for sialic acid stabilization and analysis of complex glycoprotein mixtures such as human plasma N-glycome.

Protein glycosylation is an important posttranslational modification associated, among others, with diseases and the efficacy of biopharmaceuticals. Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) can be performed to study glycosylation in a high-throughput manner, but is hampered by the instability and ionization bias experienced by sialylated glycan species. Stabilization and neutralization of these sialic acids can be achieved by permethylation or by specific carboxyl group derivatization with the possibility of discrimination between α2,3- and α2,6-linked sialic acids. However, these methods typically require relatively pure glycan samples, show sensitivity to side reactions, and need harsh conditions or long reaction times. The established method was applied to human plasma, and the analysis of the human plasma N-glycome allows highthroughput detection and relative quantitation of approx. 100 distinct N-glycan compositions with varying sialic acid linkages.

We are offering this service to academics / industrial researchers who
may have an interest in accessing this method and associated expertise within LUMC.