| Autor: |
Wood CV; Department of Chemical and Biomolecular Engineering, University of Delaware, Allan P. Colburn Laboratory, 150 Academy Street, Newark, Delaware 19716, United States., Razinkov VI; Drug Product Development, Amgen Inc., Thousand Oaks, California 91320, United States., Qi W; Drug Product Development, Amgen Inc., Thousand Oaks, California 91320, United States., Roberts CJ; Department of Chemical and Biomolecular Engineering, University of Delaware, Allan P. Colburn Laboratory, 150 Academy Street, Newark, Delaware 19716, United States., Vermant J; Department of Materials, ETH Zürich, Vladimir-Prelog-Weg 5, Zürich 8093, Switzerland., Furst EM; Department of Chemical and Biomolecular Engineering, University of Delaware, Allan P. Colburn Laboratory, 150 Academy Street, Newark, Delaware 19716, United States. |
| Abstrakt: |
When monoclonal antibodies are exposed to an air-water interface, they form aggregates, which negatively impacts their performance. Until now, the detection and characterization of interfacial aggregation have been difficult. Here, we exploit the mechanical response imparted by interfacial adsorption by measuring the interfacial shear rheology of a model antibody, anti-streptavidin immunoglobulin-1 (AS-IgG1), at the air-water interface. Strong viscoelastic layers of AS-IgG1 form when the protein is adsorbed from the bulk solution. Creep experiments correlate the compliance of the interfacial protein layer with the subphase solution pH and bulk concentration. These, along with oscillatory strain amplitude and frequency sweeps, show that the viscoelastic behavior of the adsorbed layers is that of a soft glass with interfacial shear moduli on the order of 10 -3 Pa m. Shifting the creep compliance curves under different applied stresses forms master curves consistent with stress-time superposition of soft interfacial glasses. The interfacial rheology results are discussed in the context of the interface-mediated aggregation of AS-IgG1. |
