GEN-MKT-18-7897-A
Dec 1, 2017 | Biopharma, Blogs, Life Science Research | 0 comments
The 2017 Global CESI-MS Symposium brought together KOLs and industry innovators from around the world to share their latest advancements using capillary electrophoresis integrated with electrospray ionization (CESI-MS) within the same device.
Hosted by Dr. Alexander Ivanov at the renowned Barnett Institute on the campus of Northeastern University, the 2017 Global CESI-MS Symposium was held in Boston, Massachusetts, on October 5-6, 2017.
Attendees at the conference heard how industry innovators have revealed hidden information not seen before such as proteoforms and peptides; intact mAb charge variants; native proteins; isobaric metabolites and glycans not resolved by traditional techniques; and charged and polar analytes.
The Symposium was hosted by Professor Alexander R. Ivanov, at the Barnett Institute, on the campus of Northeastern University, with sessions chaired by:
Proteomics and Metabolomics:
Novel and Advanced Applications
Biopharma
In case you were not able to attend or experience the live presentations online, we have made them available on-demand >
Join us next year in The Netherlands! Stay tuned for more information.
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.
CE‑SDS remains a cornerstone assay for characterizing fragmentation, aggregation, and product‑related impurities in therapeutic proteins. UV detection has been the long‑standing standard. However, it frequently struggles with baseline noise, limited sensitivity for minor fragments, and subjective integration.
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