protein comparability assessments and potential applicability of high throughput biophysical methods and data visualization tools to compare physical stability profiles
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2014
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Abstract
In this review, some of the challenges and opportunities encountered during protein comparability assessments are summarized with an emphasis on developing new analytical approaches to better monitor higher-order protein structures. Several case studies are presented using high throughput biophysical methods to collect protein physical stability data as function of temperature, agitation, ionic strength and/or solution pH. These large data sets were then used to construct empirical phase diagrams (EPDs), radar charts, and comparative signature diagrams (CSDs) for data visualization and structural comparisons between the different proteins. Protein samples with different sizes, post-translational modifications, and inherent stability are presented: acidic fibroblast growth factor (FGF-1) mutants, different glycoforms of an IgG1 mAb prepared by deglycosylation, as well as comparisons of different formulations of an IgG1 mAb and granulocyte colony stimulating factor (GCSF). Using this approach, differences in structural integrity and conformational stability profiles were detected under stress conditions that could not be resolved by using the same techniques under ambient conditions (i.e., no stress). Thus, an evaluation of conformational stability differences may serve as an effective surrogate to monitor differences in higher-order structure between protein samples. These case studies are discussed in the context of potential utility in protein comparability studies.
| Reference Key |
alsenaidy2014frontiersprotein
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|---|---|
| Authors | ;Mohammad A. Alsenaidy;Nishant K. eJain;Jae H. Kim;C. Russel Middaugh;David B. Volkin |
| Journal | chemical research in chinese universities |
| Year | 2014 |
| DOI |
10.3389/fphar.2014.00039
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| URL | |
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