The impact of mass spectrometry on the study of intact antibodies: from post-translational modifications to structural analysis

Publication date

2013

Authors

Thompson, N.J.ISNI 0000000125976171
Rosati, SaraISNI 000000044386241X
Rose, Richard J.
Heck, Albert J RORCID 0000-0002-2405-4404ISNI 0000000393921118

Editors

Advisors

Supervisors

Document Type

Article
Open Access logo

License

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.

Keywords

SDG 3 - Good Health and Well-being

Citation

Thompson, N J, Rosati, S, Rose, R J & Heck, A J R 2013, 'The impact of mass spectrometry on the study of intact antibodies: from post-translational modifications to structural analysis', Chemical Communications, vol. 49, no. 6, pp. 538-548. https://doi.org/10.1039/c2cc36755f