Colloidal stability is determined by the balance of repulsive and attractive intermolecular interactions between protein molecules, like a monoclonal antibody, to conserve the native folded state. Simply stated, the propensity for aggregation is reduced by less intermolecular interaction. Therefore, determination of the second virial coefficient (B22) is a valuable screening tool to predict aggregation propensity....Read More
These experiments demonstrate the utility of ARGEN™ to define oligomeric states and transitions of Human Insulin under thermal stress. Time to dimerization and time to tetramerization measurements permitted the characterization of a stable dimer species, as well as insights into the mechanisms and kinetics of higher order oligomer formation. Whereas, SEC allows the characterization of...Read More
Biopharmaceutical companies isolate many types of proteins for use in experimental and therapeutic medicines. Unfortunately, when removed from their native environments, proteins become less stable. Unstable proteins are more prone to degradation from the primary stress mechanisms: mechanical and thermal (from manufacturing, storage and transport) and biological (from drug delivery). The challenge for biopharmaceutical companies...Read More