Can I read Conformational implications of an inversed pH-dependent antibody aggregation on EtoBox?

Conformational implications of an inversed pH-dependent antibody aggregation by Natalie Perico; Judith Purtell; Thomas M. Dillon; Margaret S. Ricci is a Chemistry article available to read on EtoBox.

What is Conformational implications of an inversed pH-dependent antibody aggregation about?

Antibody formulation development relies on accelerated stability data at elevated temperatures to optimize formulation parameters. However, the pH- and temperature-dependence of aggregation is complicated for antibody formulations. In this study, a human monoclonal IgG2 antibody exhibited typical pH-dependent dimer formation under normal storage conditions (4 and/or 29 degrees C). However, an inversed pH-dependence was discovered for high molecular weight aggregate formation at elevated temperatures (37 degrees C). The different stability profiles exhibited at the various storage conditions resulted in nonlinearity of the Arrhenius kinetics. Thermal unfolding at or below 37 degrees C was not evident by differential scanning calorimetry. Enriched populations of the structural isoforms of the IgG2 subclass were tested for their unique temperature and pH-dependence of aggregation. The Arrhenius kinetics of aggregation for each of the individual IgG2 isoforms was also nonlinear. However, the temperature-dependence of clipping suggested that clip-mediated aggregation was responsible for the increased higher order aggregates at low pH and elevated temperatures. Unique clip species result

Who reads Conformational implications of an inversed pH-dependent antibody aggregation?

Author

Natalie Perico; Judith Purtell; Thomas M. Dillon; Margaret S. Ricci

Publisher

John Wiley and Sons; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0022-3549)

Published

2009

Language

EN

Field

Chemistry (Physical Sciences)