| Literature DB >> 29666888 |
Andreas Hoffmann1, Kerstin Grassl1,2, Janine Gommert1, Christian Schlesak1, Alexander Bepperling3.
Abstract
The accurate determination of protein concentration is an important though non-trivial task during the development of a biopharmaceutical. The fundamental prerequisite for this is the availability of an accurate extinction coefficient. Common approaches for the determination of an extinction coefficient for a given protein are either based on the theoretical prediction utilizing the amino acid sequence or the photometric determination combined with a measurement of absolute protein concentration. Here, we report on an improved SV-AUC based method utilizing an analytical ultracentrifuge equipped with absorbance and Rayleigh interference optics. Global fitting of datasets helped to overcome some of the obstacles encountered with the traditional method employing synthetic boundary cells. Careful calculation of dn/dc values taking glycosylation and solvent composition into account allowed the determination of the extinction coefficients of monoclonal antibodies and an Fc-fusion protein under native as well as under denaturing conditions. An intra-assay precision of 0.9% and an accuracy of 1.8% compared to the theoretical value was achieved for monoclonal antibodies. Due to the large number of data points of a single dataset, no meaningful difference between the ProteomeLab XL-I and the new Optima AUC platform could be observed. Thus, the AUC-based approach offers a precise, convenient and versatile alternative to conventional methods like total amino acid analysis (AAA).Keywords: Analytical ultracentrifugation; Biopharmaceutical; Extinction coefficient; Monoclonal antibody; Multi-signal sedimentation velocity; Refractive index increment
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Year: 2018 PMID: 29666888 DOI: 10.1007/s00249-018-1299-x
Source DB: PubMed Journal: Eur Biophys J ISSN: 0175-7571 Impact factor: 1.733