Post Doctoral Associate Institute for Bioscience and Biotechnology Research, National Institute of Standards and Technology & University of Maryland Clarksburg
Solution NMR provides a powerful way to capture protein dynamics across a wide range of timescales, offering atomic-level detail along with global insights into protein structure, size, and inter-domain motion. In this study, NMR is applied to the 50 kDa Fab domain of the NISTmAb as a model drug substance (DS) to characterize excipient-induced motions. We examine the effects of sodium chloride, sucrose, and polysorbate 80 on the local bond motions and reveal their correlation to altered Fab domain dynamics and surface accessibility. This work highlights the importance of integrating protein dynamics at all scales with HOS analyses to gain a more complete understanding of protein behavior, offering valuable insights for the development of stable biotherapeutics.
Learning Objectives:
Understand how NMR techniques can be used to study protein structure and dynamics in formulation environments.
Recognize the molecular influence of excipients such as salts, sugars, and surfactants on antibody stability.
Appreciate the role of protein dynamics data in guiding formulation innovation and enhancing biotherapeutic performance.