Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2486165 | Journal of Pharmaceutical Sciences | 2011 | 13 Pages |
Abstract
Circular dichroism (CD) spectroscopy is routinely used in the biopharmaceutical industry to study the effects of manufacturing, formulation, and storage conditions on protein conformation and stability, and these results are often included in regulatory filings. In this context, the purpose of CD spectroscopy is often to verify that a change in the formulation or manufacturing process of a product has not produced a change in the conformation of a protein. A comparison of two or more spectra is often required to confirm that the protein's structure has been maintained. Traditionally, such comparisons have been qualitative in nature, based on visually inspecting the overlaid spectra. However, visual assessment is inherently subjective and therefore prone to error. Furthermore, recent requests from regulatory agencies to demonstrate the suitability of the CD spectroscopic method for the purpose of comparing spectra have highlighted the need to appropriately qualify CD spectroscopy for characterization of biopharmaceutical protein products. In this study, we use a numerical spectral comparison approach to establish the precision of the CD spectroscopic method and to demonstrate that it is suitable for protein structural characterization in numerous biopharmaceutical applications. © 2011 WileyâLiss, Inc. and the American Pharmacists Association J Pharm Sci 100:4642-4654, 2011
Keywords
Related Topics
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Pharmacology, Toxicology and Pharmaceutical Science
Drug Discovery
Authors
Cynthia H. Li, Xichdao Nguyen, Linda Narhi, Letha Chemmalil, Edward Towers, Salman Muzammil, John Gabrielson, Yijia Jiang,