1. The impact of mass spectrometry on the study of intact antibodies: from post-translational modifications to structural analysis.
- Author
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Thompson NJ, Rosati S, Rose RJ, and Heck AJ
- Subjects
- Antibodies, Monoclonal genetics, Antibodies, Monoclonal metabolism, Antigen-Antibody Complex chemistry, Deuterium Exchange Measurement, Pharmaceutical Preparations chemistry, Pharmaceutical Preparations metabolism, Protein Processing, Post-Translational, Protein Structure, Tertiary, Recombinant Proteins biosynthesis, Recombinant Proteins chemistry, Recombinant Proteins genetics, Antibodies, Monoclonal chemistry, Mass Spectrometry
- Abstract
Monoclonal antibodies (mAbs) are important therapeutics, targeting a variety of diseases ranging from cancers to neurodegenerative disorders. In developmental stages and prior to clinical use, these molecules require thorough structural characterisation, but their large size and heterogeneity present challenges for most analytical techniques. Over the past 20 years, mass spectrometry (MS) has transformed from a tool for small molecule analysis to a technique that can be used to study large intact proteins and non-covalent protein complexes. Here, we review several MS-based techniques that have emerged for the analysis of intact mAbs and discuss the prospects of using these technologies for the analysis of biopharmaceuticals.
- Published
- 2013
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