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Macro- and Micro-Heterogeneity of Natural and Recombinant IgG Antibodies

1
Biologics CMC and developability, IRPF, Center d’immunologie Pierre Fabre, St Julien-en-Genevois CEDEX, 74160 Saint-Julien en Genevois, France
2
Anokion, 50 Hampshire Street, Suite 402, Cambridge, MA 02139, USA
*
Authors to whom correspondence should be addressed.
Antibodies 2019, 8(1), 18; https://doi.org/10.3390/antib8010018
Received: 22 December 2018 / Revised: 19 January 2019 / Accepted: 13 February 2019 / Published: 19 February 2019
(This article belongs to the Special Issue Structure and Function of Antibodies)
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PDF [281 KB, uploaded 19 February 2019]

Abstract

Recombinant monoclonal antibodies (mAbs) intended for therapeutic usage are required to be thoroughly characterized, which has promoted an extensive effort towards the understanding of the structures and heterogeneity of this major class of molecules. Batch consistency and comparability are highly relevant to the successful pharmaceutical development of mAbs and related products. Small structural modifications that contribute to molecule variants (or proteoforms) differing in size, charge or hydrophobicity have been identified. These modifications may impact (or not) the stability, pharmacokinetics, and efficacy of mAbs. The presence of the same type of modifications as found in endogenous immunoglobulin G (IgG) can substantially lower the safety risks of mAbs. The knowledge of modifications is also critical to the ranking of critical quality attributes (CQAs) of the drug and define the Quality Target Product Profile (QTPP). This review provides a summary of the current understanding of post-translational and physico-chemical modifications identified in recombinant mAbs and endogenous IgGs at physiological conditions. View Full-Text
Keywords: critical quality attributes; comparability; developability; glycosylation; quality target product profile; mass spectrometry; post-translational modifications; proteoforms; safety critical quality attributes; comparability; developability; glycosylation; quality target product profile; mass spectrometry; post-translational modifications; proteoforms; safety
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Beck, A.; Liu, H. Macro- and Micro-Heterogeneity of Natural and Recombinant IgG Antibodies. Antibodies 2019, 8, 18.

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