Automated analysis of the highly glycosylated therapeutic protein Erythropoietin via Enterprise-level data processing

Erythropoietin, commonly referred to as ‘EPO,’ is known as one of the mosts uccessful biotherapeutic drugs in history. It is a highly glycosylated glycoprotein, with 40 percent of its weight composed of sugars. EPO has important critical quality attributes like sialylation and antennary glycans, difficult to characterize by traditional approaches.

EPO serves as a good model to help develop fast analytical methods because of the large number of similarly complex molecules with heavily glycosylated species in development

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Histidine hydrogen-deuterium exchange (His-HDX) mass spectrometry for identifying protein-ligand interactions

The Byos HDX workflow makes it easy to analyze complex deuterium ratio calculations and visualize the results, helping to reduce analysis time

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Characterization of a Lysine-conjugated ADC using the Arginine-specific Protease GingisREX®

Lysine-based conjugation is a widely used non-specific conjugation strategy for the development of Antibody Drug Conjugates (ADCs) and other labelled antibody products. Conjugation at lysine residues results in highly heterogeneous products that pose challenges to current characterization methods. These challenges include accurate drug to antibody ratio (DAR) calculation, site-specific localization of modified lysine residues as well as quantification of site occupancy.

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Automated Spectrum Annotation and Structure Disambiguation of Released N-linked Glycans

Monosaccharide composition is often discernible directly from accurate molecular mass (MS1); however, topology (monosaccharide connectivity) requires MS2, and glycosidic linkage information and anomericity requires, at least, MS3 if not combined with orthogonal insights. Here we report on disambiguation of topological isomers directly from tandem MS spectra.

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Optimization of a Liquid Chromatography-Tandem Mass Spectrometry mRNA Sequence Mapping Workflow

In this study we investigate the primary structure of an eGFP mRNA sequence (RiboPro) using a novel oligonucleotide mapping workflow

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