Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry.

ABSTRACT: Protein function is dictated by protein conformation. For the protein biopharmaceutical industry, therefore, it is important to have analytical tools that can detect changes in protein conformation rapidly, accurately, and with high sensitivity. In this paper we show that hydrogen/deuterium exchange mass spectrometry (H/DX-MS) can play an important role in fulfilling this need within the industry. H/DX-MS was used to assess both global and local conformational behavior of a recombinant monoclonal IgG1 antibody, a major class of biopharmaceuticals. Analysis of exchange into the intact, glycosylated IgG1 (and the Fab and Fc regions thereof) showed that the molecule was folded, highly stable, and highly amenable to analysis by this method using less than a nanomole of material. With improved

SUBMITTER: Houde D 

PROVIDER: S-EPMC2779575 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature