Poster- SUPR-CM for Improved Measurements of Antibody Stability
Summary: Establishing the stability of monoclonal antibodies is an important measurement within biologic drug development. Currently, thermal approaches like differential scanning fluorimetry (DSF) and differential scanning calorimetry (DSC) are often preferred despite drawbacks like non-equilibrium measurements and thermal alteration of solvent conditions. Chemical denaturation has the advantage of reversible, equilibrated measurement of protein stability. However, factors including slow measurement time, low throughput, low quality of data and high sample usage limit the incorporation of chemical denaturation within the development process. Here we present stability information from forced degradation studies on a monoclonal antibody. Chemical denaturation experiment where performed with the SUPR-CM fluorescence plate reader and demonstrate the instruments ability to acquire chemical denaturation stability information quickly, and with little sample, while not compromising on the quality of the measurement data.
