GEN-MKT-18-7897-A
Nov 9, 2016 | Biopharma, Blogs | 0 comments
A variety of post-translational modifications (PTMs) can impact a biotherapeutic protein’s mass, but none are as common as glycosylation.[1] Hence, the headline for a recent article in Genetic Engineering and Biotechnology News, “Post-Translational Icing on the Biologics Cake,” featuring comments from Sean McCarthy, Ph.D., Global Market Manager of Biologics at SCIEX.
About the Article: Biotherapeutic protein glycosylation plays a key role in whether or not a biologic drug can effectively treat disease, making the detection and characterization of these glycan structures an important topic for pharmaceutical developers. Dr. McCarthy gives his take on using different liquid chromatography separation techniques together with mass spectrometry to go after low-level immunogenic glycan epitopes on biotherapeutics, which could elicit an undesirable immune response in patients. The development of focused instrumentation and software solutions to meet the needs of biologics characterization workflows are profiled in this article, with a focus on the SCIEX TripleTOF® 6600 MS system coupled with BioPharmaView™ software. Together, the TripleTOF system and BioPharmaView software can profile intact protein glycoforms, or comprehensively identify and quantitate specific glycopeptides.Read the Article >
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About Dr. McCarthy:Sean M. McCarthy received his degree in Chemistry from the University of Vermont in 2005, followed by his NIH postdoctoral associate within the Department of Pathology at the same institution. His work centered on environmental oxidative stress related diseases using a variety of biochemical and mass spectrometric techniques. Dr. McCarthy has worked in the mass spectrometry industry since 2008 and has held several scientific and business development positions to address pharmaceutical and biopharmaceutical characterization. Dr. McCarthy is currently the Global Market Manager of Biologics at SCIEX, where his focus is on delivering targeted solutions for biopharmaceutical characterization.
[1] http://www.sciencedirect.com/science/article/pii/S135964461600026X
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As an analytical strategy, middle-down mass spectrometry (MS) workflows characterize biotherapeutic proteins by analyzing large, digested protein fragments or defined subunits, rather than fully intact proteins (top-down) or digested peptides (bottom-up). A middle-down strategy combines the strengths of top-down and bottom-up approaches by delivering high sequence coverage and structural specificity while maintaining relatively simple sample preparation. In practice, middle-down analysis enables accurate mass measurement, rapid sequence confirmation, and localization of key post-translational modifications (PTMs) on protein subunits that are directly relevant to product quality.
In biopharmaceutical development, sequence variants (SV) are considered an inherent risk of producing complex proteins in living systems. Sequence variants are unintended changes to the amino acid sequence of a biotherapeutic and can be caused by errors in transcription or translation in the host cell, or cell culture and process conditions. Detailed analysis of SVs is important in process and product development to ensure the drug’s safety and efficacy. Even low‑level sequence variants can have significant implications for product quality, safety, and efficacy, making their accurate detection and characterization a critical requirement across development, process optimization, and regulatory submission.
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