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Mass spectrometry for the biophysical characterization of therapeutic monoclonal antibodies
Author(s) -
Zhang Hao,
Cui Weidong,
Gross Michael L.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.11.027
Subject(s) - monoclonal antibody , characterization (materials science) , chemistry , mass spectrometry , computational biology , folding (dsp implementation) , peptide , antibody , biophysics , nanotechnology , biochemistry , biology , chromatography , materials science , immunology , engineering , electrical engineering
Monoclonal antibodies (mAbs) are powerful therapeutics, and their characterization has drawn considerable attention and urgency. Unlike small‐molecule drugs (150–600 Da) that have rigid structures, mAbs (∼150 kDa) are engineered proteins that undergo complicated folding and can exist in a number of low‐energy structures, posing a challenge for traditional methods in structural biology. Mass spectrometry (MS)‐based biophysical characterization approaches can provide structural information, bringing high sensitivity, fast turnaround, and small sample consumption. This review outlines various MS‐based strategies for protein biophysical characterization and then reviews how these strategies provide structural information of mAbs at the protein level (intact or top‐down approaches), peptide, and residue level (bottom‐up approaches), affording information on higher order structure, aggregation, and the nature of antibody complexes.