Protein-protein interactions investigated by DLS
The University of Applied Sciences Kaiserslautern
Controlling protein-protein interactions is vital for highly concentrated formulations of therapeutic proteins, as they impact stability as well as viscosity. This article presents high-throughput screening of these interactions using the DynaPro Plate Reader. Rather than a complex, rigorous characterization, the author demonstrated how simple indicators such as the diffusion interaction parameter kD (moderate concentrations up to 12 mg/mL) and the apparent change in hydrodynamic radius R/Rh with concentration (at 150 mg/mL) are useful for understanding behavior. These parameters showed clear trends with pH and ionic strength that were expected based on electrostatic considerations.