The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals
Abstract
Therapeutic proteins produced using recombinant DNA technologies are generally complex, heterogeneous, and subject to a variety of enzymatic or chemical modifications during expression, purification, and long‐term storage. The use of mass spectrometry (MS) for the evaluation of recombinant protein sequence and structure provides detailed information regarding amino acid modifications and sequence alterations that have the potential to affect the safety and activity of therapeutic protein products. General MS approaches for the characterization of recombinant therapeutic protein products will be reviewed with particular attention given to the standard MS tools available in most biotechnology laboratories. A number of recent examples will be used to illustrate the utility of MS strategies for evaluation of recombinant protein heterogeneity resulting from post‐translational modifications (PTMs), sequence variations generated from proteolysis or transcriptional/translational errors, and degradation products which are formed during processing or final product storage. Specific attention will be given to the MS characterization of monoclonal antibodies as a model system for large, glycosylated, recombinant proteins. Detailed examples highlighting the use of MS for the analysis of monoclonal antibody glycosylation, deamidation, and disulfide mapping will be used to illustrate the application of these techniques to a wide variety of heterogeneous therapeutic protein products. The potential use of MS to support the selection of cell line/clone selection and formulation development for therapeutic antibody products will also be discussed. © 2007 Wiley Periodicals, Inc., Mass Spec Rev
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Cites
Electrospray Ionization for Mass Spectrometry of Large Biomolecules
Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., & Whitehouse, C. M. (1989) · Science · doi:10.1126/science.2675315 · Cited by 7,634
Cited by
PEGylation of therapeutic proteins
Jevševar, S., Kunstelj, M., & Porekar, V. G. (2010) · Biotechnology Journal · doi:10.1002/biot.200900218 · Cited by 681
HILIC analysis of fluorescence-labeled N-glycans from recombinant biopharmaceuticals
Melmer, M., Stangler, T., Schiefermeier, M., Brunner, W., Toll, H., Rupprechter, A., Lindner, W., & Premstaller, A. (2010) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-010-3988-x · Cited by 104
Haselberg, R., De Vijlder, T., Heukers, R., Smit, M. J., Romijn, E. P., Somsen, G. W., & Domínguez-Vega, E. (2018) · Analytica Chimica Acta · doi:10.1016/j.aca.2018.08.024 · Cited by 64
Dominguez-Vega, E., De Vijlder, T., Romijn, E. P., & Somsen, G. W. (2017) · Analytica Chimica Acta · doi:10.1016/j.aca.2017.06.021 · Cited by 19
Naumann, L., Schlossbauer, P., Klingler, F., Hesse, F., Otte, K., & Neusüß, C. (2022) · Journal of Separation Science · doi:10.1002/jssc.202100865 · Cited by 18
Metadata
- Authors
- Srebalus Barnes, C. A., & Lim, A.
- Venue
- Mass Spectrometry Reviews
- Publisher
- Wiley
- Published
- 2007-04-04
- Volume
- 26
- Issue
- 3
- Pages
- 370-388
- ISSN
- 0277-7037 (ISSN-L)
- 1098-2787
- OpenAlex
- W1999139162
- Cited by
- 175
- References
- 1
- FWCI
- 5.81
- Type
- journal article
- Language
- en
- Open access
- closed
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