期刊
FEBS LETTERS
卷 588, 期 2, 页码 308-317出版社
WILEY
DOI: 10.1016/j.febslet.2013.11.027
关键词
Monoclonal antibody; Mass spectrometry; Native ESI; Top-down and bottom-up; Protein footprinting; Hydrogen/deuterium exchange; FPOP; Ion mobility
资金
- National Institute of General Medical Sciences of the US National Institutes of Health [P41 GM103422-35]
- Photosynthetic Antenna Research Center, an Energy Frontier Research Center
- U.S. DOE, Office of Basic Energy Sciences [DE-SC 0001035]
- DOE
- NIH
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 (similar to 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. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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