| Literature DB >> 27527097 |
Richard Y-C Huang1, Roxana E Iacob2, Stanley R Krystek3, Mi Jin4, Hui Wei5, Li Tao5, Tapan K Das5, Adrienne A Tymiak1, John R Engen2, Guodong Chen6.
Abstract
Aggregation of protein therapeutics has long been a concern across different stages of manufacturing processes in the biopharmaceutical industry. It is often indicative of aberrant protein therapeutic higher-order structure. In this study, the aggregation propensity of a human Fc-fusion protein therapeutic was characterized. Hydrogen/deuterium exchange mass spectrometry (HDX-MS) was applied to examine the conformational dynamics of dimers collected from a bioreactor. HDX-MS data combined with spatial aggregation propensity calculations revealed a potential aggregation interface in the Fc domain. This study provides a general strategy for the characterization of the aggregation propensity of Fc-fusion proteins at the molecular level.Graphical Abstract.Entities:
Keywords: Aggregation propensity; Fc fusion protein; Hydrogen/Deuterium exchange mass spectrometry
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Year: 2016 PMID： 27527097 DOI： 10.1007/s13361-016-1452-7
Source DB: PubMed Journal: J Am Soc Mass Spectrom ISSN： 1044-0305 Impact factor: 3.109