A new tool for monoclonal antibody analysis: application of IdeS proteolysis in IgG domain-specific characterization.

ABSTRACT: Monoclonal antibody (mAb) products are extraordinarily heterogeneous due to the presence of a variety of enzymatic and chemical modifications, such as deamidation, isomerization, oxidation, glycosylation, glycation, and terminal cyclization. The modifications in different domains of the antibody molecule can result in different biological consequences. Therefore, characterization and routine monitoring of domain-specific modifications are essential to ensure the quality of the therapeutic antibody products. For this purpose, a rapid and informative methodology was developed to examine the heterogeneity of individual domains in mAb products. A recently discovered endopeptidase, IdeS, cleaves heavy chains below the hinge region, producing F(ab') 2 and Fc fragments. Following reduction of dis

SUBMITTER: An Y 

PROVIDER: S-EPMC4171023 | biostudies-literature | 2014 Jul-Aug

REPOSITORIES: biostudies-literature