Advances in affinity ligand-functionalized nanomaterials for biomagnetic separation

ABSTRACT The downstream processing of proteins remains the most significant cost in protein production, and is largely attributed to rigorous chromatographic purification protocols, where the stringency of purity for biopharmaceutical products sometimes exceeds 99%. With an ever burgeoning biotechno...

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Veröffentlicht in:Biotechnology and bioengineering 2016-01, Vol.113 (1), p.11-25
Hauptverfasser: Fields, Conor, Li, Peng, O'Mahony, James J., Lee, Gil U.
Format: Artikel
Sprache:eng
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Zusammenfassung:ABSTRACT The downstream processing of proteins remains the most significant cost in protein production, and is largely attributed to rigorous chromatographic purification protocols, where the stringency of purity for biopharmaceutical products sometimes exceeds 99%. With an ever burgeoning biotechnology market, there is a constant demand for alternative purification methodologies, to ameliorate the dependence on chromatography, while still adhering to regulatory concerns over product purity and safety. In this article, we present an up‐to‐date view of bioseparation, with emphasis on magnetic separation and its potential application in the field. Additionally, we discuss the economic and performance benefits of synthetic ligands, in the form of peptides and miniaturized antibody fragments, compared to full‐length antibodies. We propose that adoption of synthetic affinity ligands coupled with magnetic adsorbents, will play an important role in enabling sustainable bioprocessing in the future. Biotechnol. Bioeng. 2016;113: 11–25. © 2015 Wiley Periodicals, Inc. Magnetic separation, in combination with adoption of synthetic affinity ligands, offers an alternative approach to protein purification and has the potential to alleviate bottleneck issues associated with industrial‐scale downstream chromatographic purification. This review article focuses on magnetic bioseparation, with emphasis on the economic and performance benefits of peptides and antibody fragments, as alternative, synthetic affinity ligand reagents to full‐length antibodies.
ISSN:0006-3592
1097-0290
DOI:10.1002/bit.25665