Modification of the kinetic stability of immunoglobulin G by solvent additives.

ABSTRACT: Biophysical properties of antibody-based biopharmaceuticals are a critical part of their release criteria. In this context, finding the appropriate formulation is equally important as optimizing their intrinsic biophysical properties through protein engineering, and both are mutually dependent. Most previous studies have empirically tested the impact of additives on measures of colloidal stability, while mechanistic aspects have usually been limited to only the thermodynamic stability of the protein. Here we emphasize the kinetic impact of additives on the irreversible denaturation steps of immunoglobulins G (IgG) and their antigen-binding fragments (Fabs), as these are the key committed steps preceding aggregation, and thus especially informative in elucidating the molecular parameters of

SUBMITTER: Schaefer JV 

PROVIDER: S-EPMC5973700 | biostudies-literature | 2018 May/Jun

REPOSITORIES: biostudies-literature