A prerequisite for a successful biotherapeutic formulation is one where the protein is stable and correctly folded. The new technique of dynamic multi-mode spectroscopy (DMS) was used to study the stability of a monoclonal antibody biotherapeutic formulated in acetate and lactate buffers. The samples were measured several times over a period of weeks and it became apparent that the antibody behaved differently as it aged in the two formulations, with the lactate formulation imparting greater robustness than the acetate.
