ACCESS MONOCLONAL ANTIBODY QUALITY ATTRIBUTES WITH HRMS ANALYTICAL POWER
Speaker: Ricardo Gomes
Senior research associate at the Mass Spectrometry unit of iBET
SHORT BIO: Ricardo Gomes is a biochemist with a doctorate in biochemistry regulation from the University of Lisbon, Faculty of Sciences. His doctorate focused on the biochemistry effects of protein glycation, post-translational modification, protein structure, and the folding/misfolding balance. This work was expanded in his post-doctoral studies where he investigated the biochemical effects at the cellular levels of glycation-induced protein misfolding using MS-based approaches. This work gave him solid and significant expertise in the field of mass-spectrometry and proteomics using several MS and LC systems. Since 2015, Dr. Gomes has been a senior research associate at the mass spectrometry unit of iBET in Portugal. iBET is a private non-profit research-intensive institution and as Biotechnology Research Organisation, iBET acts as an interface between academic institutions while also creating and organizing autonomous knowledge and expertise. In the mass spectrometry facility at iBET, Dr. Gomes is particularly focused on the biologics characterization, namely, multiple attribute methodology, host cell protein analysis, and SWATH workflows. Dr. Gomes is the author of 28 scientific articles and 4 book chapters.
EVENT OVERVIEW: The fast pace and growing demand for therapeutic monoclonal antibodies (mAbs) is forcing clinical and manufacturing processes to evolve to meet safety and efficiency requirements. Comprehensive characterization at the molecular level of antibodies heterogeneity such as glycoforms, post-translational modifications, and sequence variations is of utmost importance. In the webcast, learn how a high-resolution mass spectrometry (MS)-based approach can be a powerful analytical strategy to monitor and define multiple critical quality attributes (multi-attribute methodology) of complex biomolecules in a single assay using a single instrument platform.
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