Journal article
A Thermal-Cycling Method for Disaggregating Monoclonal Antibody Oligomers
Abstract
Non-native oligomeric forms of biopharmaceutical proteins are therapeutically inactive, and potentially toxic and immunogenic, and therefore undesirable in pharmaceutical formulations. Immunoglobulin G class of antibodies are known to form stable nonnative oligomers through Fab-Fab interactions. In this paper, we investigate thermal-cycling as a technique for disaggregating antibody oligomers. Aggregate containing monoclonal antibody (mAb) …
Authors
Sadavarte RH; Ghosh R
Journal
Journal of Pharmaceutical Sciences, Vol. 103, No. 3, pp. 870–878
Publisher
Elsevier
Publication Date
March 2014
DOI
10.1002/jps.23863
ISSN
1520-6017
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Antibodies, MonoclonalCD4 AntigensCircular DichroismDimerizationDrug StabilityDrug StorageHot TemperatureHumansHydrophobic and Hydrophilic InteractionsImmunoglobulin Fab FragmentsImmunoglobulin GModels, MolecularParticle SizeProtein Interaction Domains and MotifsProtein RefoldingProtein StabilityProtein Structure, SecondaryProtein UnfoldingRecombinant ProteinsSolubility