Investigation of monoclonal antibody dimers in a final formulated drug by separation techniques coupled to native mass spectrometry.

ABSTRACT: Therapeutic monoclonal antibodies (mAbs) are highly complex proteins that must be exhaustively characterized according to the regulatory authorities' recommendations. MAbs display micro-heterogeneity mainly due to their post-translational modifications, but also to their susceptibility to chemical and physical degradations. Among these degradations, aggregation is quite frequent, initiated by protein denaturation and then dimer formation. Here, we investigated the nature and structure of the high molecular weight species (HMW) present at less than 1% in an unstressed formulated roledumab biopharmaceutical, as a model of high purity mAb. HMW species were first purified through preparative size-exclusion chromatography (SEC) and then analyzed by a combination of chromatographic methods (ion-

SUBMITTER: Rouby G 

PROVIDER: S-EPMC7531515 | biostudies-literature | 2020 Jan-Dec

REPOSITORIES: biostudies-literature