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Cytotechnology

, Volume 53, Issue 1–3, pp 121–125 | Cite as

Modifications of therapeutic proteins: challenges and prospects

  • Nigel Jenkins
NICB special Issue

Abstract

The production of therapeutic proteins is one of the fastest growing sectors of the pharmaceutical industry. However, most proteins used in drug therapy require complex post-translational modifications for efficient secretion, drug efficacy and stability. Common protein modifications include variable glycosylation, misfolding and aggregation, oxidation of methionine, deamidation of asparagine and glutamine, and proteolysis. These modifications not only pose challenges for accurate and consistent bioprocessing, but also may have consequences for the patient in that incorrect modifications or aggregation may lead to an immune response to the protein therapeutic. This review provides examples of analytical and preventative advances that have been devised to meet these challenges, and insights into how further advances can improve the efficiency and safety in manufacturing recombinant proteins.

Keywords

Recombinant protein Cell culture Aggregation Folding Oxidation Deamidation Glycosylation Therapeutics 

Abbreviations

ADCC

antibody-dependent cellular cytotoxicity

CHO

Chinese hamster ovary

EPO

erythropoietin

ESI-MS

electrospray ionization mass spectrometry

HPLC

high pressure liquid chromatography

MALDI

matrix-assisted laser desorption-ionization

PTM

post-translational modification

UDP

uridine-5′-diphosphate

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Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  1. 1.National Institute for Bioprocessing Research and TrainingUniversity College DublinBelfield, DublinIreland

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