modification of proteins. In short, protein stabilization is major challenge with no universal solution. Consideration of the pathways of thermal protein deactivation shows that irreversible aggregation, rather than chemical degradation or unfolding is the primary mechanism for loss of activity. For example, simple mechanical stimulation (shaking) of insulin leads to aggregation into amyloidtype fibers and loss of efficacy and bioavailability and the gene therapy Zolgensma™ has just a 14-day shelf life, cannot be agitated, and must be retained between 2 and 8°C. Clearly, this is a barrier to wider use. Aggregation of recombinant human interferon beta (rhIFN-b) leads to immunogenicity for patients with multiple sclerosis. Emerging antibody-based therapies have a major problem with aggregation at all stages of their life cycle, necessitating complex formulation processes.