LAPSE:2023.5945
Published Article
LAPSE:2023.5945
Protein L—More Than Just an Affinity Ligand
February 23, 2023
Abstract
In the past 30 years, highly specific drugs, known as antibodies, have conquered the biopharmaceutical market. In addition to monoclonal antibodies (mAbs), antibody fragments are successfully applied. However, recombinant production faces challenges. Process analytical tools for monitoring and controlling production processes are scarce and time-intensive. In the downstream process (DSP), affinity ligands are established as the primary and most important step, while the application of other methods is challenging. The use of these affinity ligands as monitoring tools would enable a platform technology to monitor process steps in the USP and DSP. In this review, we highlight the current applications of affinity ligands (proteins A, G, and L) and discuss further applications as process analytical tools.
In the past 30 years, highly specific drugs, known as antibodies, have conquered the biopharmaceutical market. In addition to monoclonal antibodies (mAbs), antibody fragments are successfully applied. However, recombinant production faces challenges. Process analytical tools for monitoring and controlling production processes are scarce and time-intensive. In the downstream process (DSP), affinity ligands are established as the primary and most important step, while the application of other methods is challenging. The use of these affinity ligands as monitoring tools would enable a platform technology to monitor process steps in the USP and DSP. In this review, we highlight the current applications of affinity ligands (proteins A, G, and L) and discuss further applications as process analytical tools.
Record ID
Keywords
affinity ligands, antibody fragments, monoclonal antibodies, process analytical technology, protein A, protein G, protein L
Subject
Suggested Citation
Kittler S, Besleaga M, Ebner J, Spadiut O. Protein L—More Than Just an Affinity Ligand. (2023). LAPSE:2023.5945
Author Affiliations
Kittler S: Research Division Integrated Bioprocess Development, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, Gumpendorfer Strasse 1a, 1060 Vienna, Austria; Alfred Gruber GmbH, Nordstrasse 6, 5301 Eugendorf, Austria
Besleaga M: Research Division Integrated Bioprocess Development, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, Gumpendorfer Strasse 1a, 1060 Vienna, Austria
Ebner J: Research Division Integrated Bioprocess Development, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, Gumpendorfer Strasse 1a, 1060 Vienna, Austria; Alfred Gruber GmbH, Nordstrasse 6, 5301 Eugendorf, Austria
Spadiut O: Research Division Integrated Bioprocess Development, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, Gumpendorfer Strasse 1a, 1060 Vienna, Austria [ORCID]
Besleaga M: Research Division Integrated Bioprocess Development, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, Gumpendorfer Strasse 1a, 1060 Vienna, Austria
Ebner J: Research Division Integrated Bioprocess Development, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, Gumpendorfer Strasse 1a, 1060 Vienna, Austria; Alfred Gruber GmbH, Nordstrasse 6, 5301 Eugendorf, Austria
Spadiut O: Research Division Integrated Bioprocess Development, Institute of Chemical, Environmental and Bioscience Engineering, TU Wien, Gumpendorfer Strasse 1a, 1060 Vienna, Austria [ORCID]
Journal Name
Processes
Volume
9
Issue
5
First Page
874
Year
2021
Publication Date
2021-05-17
ISSN
2227-9717
Version Comments
Original Submission
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PII: pr9050874, Publication Type: Review
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Published Article
LAPSE:2023.5945
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https://doi.org/10.3390/pr9050874
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Feb 23, 2023
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