The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Silicone Oil- and Agitation-Induced Aggregation of a Monoclonal Antibody in Aqueous Solution
Open accessAbstract
Silicone oil, which is used as a lubricant or coating in devices such as syringes, needles and pharmaceutical containers, has been implicated in aggregation and particulation of proteins and antibodies. Aggregation of therapeutic protein products induced by silicone oil can pose a challenge to their development and commercialization. To systematically characterize the role of silicone oil on protein aggregation, the effects of agitation, temperature, pH and ionic strength on silicone oil-induced loss of monomeric anti-streptavidin IgG 1 antibody were examined. Additionally, the influences of excipients polysorbate20 and sucrose on protein aggregation were investigated. In the absence of agitation, protein absorbed to silicone oil with approximately monolayer coverage, however silicone oil did not stimulate aggregation during isothermal incubation unless samples were also agitated. A synergistic stimulation of aggregation by a combination of agitation and silicone oil was observed. Solution conditions which reduced colloidal stability of the antibody, as assessed by determination of osmotic second virial coefficients, accelerated aggregation during agitation with silicone oil. Polysorbate20 completely inhibited silicone oil-induced monomer loss during agitation. A formulation strategy optimizing colloidal stability of the antibody as well as incorporation of surfactants such as polysorbate20 is proposed to reduce silicone oil-induced aggregation of therapeutic protein products.
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Cites
Chi, E. Y., Krishnan, S., Randolph, T. W., & Carpenter, J. F. (2003) · Pharmaceutical Research · doi:10.1023/a:1025771421906 · Cited by 1,379
Self-citationEffects of protein aggregates: An immunologic perspective
Rosenberg, A. S. (2006) · The AAPS Journal · doi:10.1208/aapsj080359 · Cited by 1,355
Protein secondary structures in water from second-derivative amide I infrared spectra
Dong, A., Huang, P., & Caughey, W. S. (1990) · Biochemistry · doi:10.1021/bi00465a022 · Cited by 1,333
The stabilization of proteins by sucrose.
Lee, J. C., & Timasheff, S. N. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68947-7 · Cited by 1,112
Monoclonal antibody successes in the clinic
Reichert, J. M., Rosensweig, C. J., Faden, L. B., & Dewitz, M. C. (2005) · Nature Biotechnology · doi:10.1038/nbt0905-1073 · Cited by 733
Predicting protein crystallization from a dilute solution property
George, A., & Wilson, W. W. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994001216 · Cited by 608
Sluzky, V, Tamada, J. A., Klibanov, A. M., & Langer, R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.21.9377 · Cited by 513
Chi, E. Y., Krishnan, S., Kendrick, B. S., Chang, B. S., Carpenter, J. F., & Randolph, T. W. (2003) · Protein Science · doi:10.1110/ps.0235703 · Cited by 343
Self-citationEffects of Tween 20® and Tween 80® on the Stability of Albutropin During Agitation
Chou, D. K., Krishnamurthy, R., Randolph, T. W., Carpenter, J. F., & Manning, M. C. (2005) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.20365 · Cited by 307
Self-citationBam, N. B., Cleland, J. L., Yang, J. G., Manning, M. C., Carpenter, J. F., Kelley, R. F., & Randolph, T. W. (1998) · Journal of Pharmaceutical Sciences · doi:10.1021/js980175v · Cited by 286
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Cited by
Physicochemical Stability of Monoclonal Antibodies: A Review
Le Basle, Y., Chennell, P., Tokhadze, N., Astier, A., & Sautou, V. (2020) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2019.08.009 · Cited by 429
Strategies for the assessment of protein aggregates in pharmaceutical biotech product development
den Engelsman, J., Garidel, P., Smulders, R., Koll, H., Smith, B., Bassarab, S., Seidl, A., Hainzl, O., & Jiskoot, W. (2011) · Pharmaceutical Research · doi:10.1007/s11095-010-0297-1 · Cited by 348
Liu, L., Ammar, D. A., Ross, L. A., Mandava, N., Kahook, M. Y., & Carpenter, J. F. (2011) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.10-6431 · Cited by 199
Self-citationProtein Aggregation and Particle Formation in Prefilled Glass Syringes
Gerhardt, A., Mcgraw, N. R., Schwartz, D. K., Bee, J. S., Carpenter, J. F., & Randolph, T. W. (2014) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.23973 · Cited by 197
Self-citationEffects of Syringe Material and Silicone Oil Lubrication on the Stability of Pharmaceutical Proteins
Krayukhina, E., Tsumoto, K., Uchiyama, S., & Fukui, K. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24184 · Cited by 158
Metadata
- Authors
- Thirumangalathu, R., Krishnan, S., Ricci, M. S., Brems, D. N., Randolph, T. W., & Carpenter, J. F.
- Venue
- Journal of Pharmaceutical Sciences
- Publisher
- Elsevier BV
- Published
- 2009-09
- Volume
- 98
- Issue
- 9
- Pages
- 3167-3181
- ISSN
- 0022-3549 (ISSN-L)
- OpenAlex
- W2106357609
- Cited by
- 294
- References
- 22
- FWCI
- 6.84
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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