(128c) Antibody Adsorption on Fluid-Fluid Interface

Many proteins will adsorb on fluid-fluid interfaces and dynamically unfold. This tendency causes multiple problems in the formulations steps for biomacromolecules in the pharmaceutical industry, which is actively working on developing protein-based drugs. To resolve this issue, it is necessary to study the rate of antibody adsorption on the interface, using air-water interface as an example. We propose to examine Immunoglobulin 1 (IgG1) as a model antibody, and we will examine Bovine Serum Albumin (BSA) in physiologically relevant solvents as a ‘control’ protein. Circular Dichroism spectrometer will be used to test BSA’s stability at different temperatures ranging from room temperature to 90⁰C, using water bath. The heating and cooling curves will let us determine the BSA’s melting point and help to predict the reversibility nature of the protein, if any. Another set of experiments using pendant drop tensiometry technique helps to determine BSA’s surface tension and critical micelle concentration using water, NaCl, and surfactants as excipients. This will provide us with enough information to make conclusions about BSA’s adsorption properties on the interface. Similar set of experiments would be done using IgG1-excipient mixture to determine its adsorption properties using CD spectroscopy and pendant drop tensiometer. The above studies will allow us to predict the physical stability of the protein antibodies and to define manufacturing conditions biomacromolecules involved in autoimmune diseases and cancer treatments.