BIOT 136 |
| Recombinant therapeutic monoclonal antibodies are subject to a variety of physical and chemical modifications that may affect their bioactivities. Protein degradation reactions include but not limited to aggregation, clipping, oxidation, deamidation, proteolysis cleavage, disulfide-bond scrambling, glycosylation and cyclization. These degradation reactions create size, charge, or preferred conformation heterogeneity, which may further influence their binding or neutralizing capability against their targets. The potential impact of these modifications depends on not only their nature but also the site. Our characterization works on various degradation products revealed the locations and the extent of the degradations. Together with corresponding bioassay results, the findings allowed us to attain a better appreciation of their relationships. These data were collected throughout the commercial formulation development process of an IgG2. |
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Biophysical and Biomolecular Symposium: Protein Chemical Instability
8:00 AM-11:05 AM, Tuesday, August 21, 2007 BCEC -- 106, Oral
Division of Biochemical Technology |