Potential inaccurate quantitation and sizing of protein aggregates by size exclusion chromatography: essential need to use orthogonal methods to assure the quality of therapeutic protein products
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Aggregates of capsids represent another product-related impurity with detrimental impact on safety and long-term stability of the vector product, as even trace amounts below 1% provide nucleation sites for further aggregation.
“Aggregates of capsids, as the third potential CQA, represent another product-related impurity with detrimental impact on safety and long-term stability of the vector product, as even trace amounts (e.g., <1%) provide nucleation sites for further aggregation.28,44,45”
From Analytical methods for process and product characterization of recombinant adeno-associated virus-based gene therapies (2021) · cites this paper as [44]
AUC is well suited as an orthogonal method to validate more rapid methods with poorer resolution.
“Instead, it is well suited as an orthogonal method to validate more rapid methods with poorer resolution.”
From Analytical methods for process and product characterization of recombinant adeno-associated virus-based gene therapies (2021) · cites this paper as [44]
AUC throughput is limited to 7 samples in around 6 h, making routine use in process development challenging.
“With throughput limited to 7 samples in around 6 h, routine use of AUC in process development is challenging.”
From Analytical methods for process and product characterization of recombinant adeno-associated virus-based gene therapies (2021) · cites this paper as [44]
SEC-based methods are generally more accurate and precise than orthogonal methods such as AUC or DLS, but accuracy for large aggregates is limited by filtration, nonspecific interactions, and dissociation of reversible aggregates.
“They are generally more accurate and precise than orthogonal methods, e.g., AUC or DLS, but accuracy for large aggregates is limited by the SEC separation mechanism: filtration of aggregates by the stationary phase, nonspecific interactions between aggregates and the column frit, and dissociation of reversible aggregates due to dilution in the mobile phase are common.”
From Analytical methods for process and product characterization of recombinant adeno-associated virus-based gene therapies (2021) · cites this paper as [44]
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Self-citation
- Authors
- Carpenter, J. F., Randolph, T. W., Jiskoot, W., Crommelin, D. J. A., Middaugh, C. R., & Winter, G.
- Affiliations
- University of Colorado Anschutz (US)
- University of Colorado Boulder (US)
- Leiden University (NL)
- Utrecht University (NL)
- University of Kansas (US)
- Ludwig-Maximilians-Universität München (DE)
- Corresponding author
- Carpenter, John F.
- Venue
- Journal of Pharmaceutical Sciences
- Publisher
- Elsevier BV
- Published
- 2010-05
- Volume
- 99
- Issue
- 5
- Pages
- 2200-2208
- ISSN
- 0022-3549 (ISSN-L)
- OpenAlex
- W2106907072
- Cited by
- 202
- References
- 43
- Citations by year
- 2026: 4 · 2025: 2 · 2023: 4 · 2022: 8 · 2021: 11 · 2020: 10 · 2019: 10 · 2018: 22 · 2017: 9 · 2016: 12 · 2015: 21 · 2014: 18 · 2013: 20 · 2012: 26
- FWCI
- 6.37
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Pharmaceutical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Immunology and Microbiology › Immunology › Biosimilars and Bioanalytical Methods
- Physical Sciences › Chemistry › Analytical Chemistry › Analytical Methods in Pharmaceuticals
- Keywords
- protein aggregates, size exclusion chromatography, therapeutic proteins, protein stability, immunogenicity, protein degradation products, injection site reactions, anaphylaxis
- MeSH terms
- Chromatography, Gel, Drug Stability, Pharmaceutical Preparations, Quality Control, Recombinant Proteins, Protein Stability
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