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Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces.
Open accessAbstract
The stability of protein-based pharmaceuticals (e.g., insulin) is important for their production, storage, and delivery. To gain an understanding of insulin's aggregation mechanism in aqueous solutions, the effects of agitation rate, interfacial interactions, and insulin concentration on the overall aggregation rate were examined. Ultraviolet absorption spectroscopy, high-performance liquid chromatography, and quasielastic light scattering analyses were used to monitor the aggregation reaction and identify intermediate species. The reaction proceeded in two stages; insulin stability was enhanced at higher concentration. Mathematical modeling of proposed kinetic schemes was employed to identify possible reaction pathways and to explain greater stability at higher insulin concentration.
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Cited by
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Mann, J. L., Maikawa, C. L., Smith, A. A. A., Grosskopf, A. K., Baker, S. W., Roth, G. A., Meis, C. M., Gale, E. C., Liong, C. S., Correa, S., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aba6676 · Cited by 62
Metadata
- Authors
- Sluzky, V, Tamada, J. A., Klibanov, A. M., & Langer, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1991-11
- Volume
- 88
- Issue
- 21
- Pages
- 9377-9381
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1988089792
- Cited by
- 513
- References
- 0
- FWCI
- 1.78
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. https://app.cochat.ai/papers/10.1073/pnas.88.21.9377
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- Sluzky, V, Tamada, J. A., Klibanov, A. M., & Langer, R. (1991). Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.88.21.9377
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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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