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Conventional pharmaceutical protein stabilization approaches use sugar based excipients to encase the proteins in glassy state structures by drying (freeze dry, spray dry, etc.), thus providing a more rigid, thermodynamically stable state. Recent neutron scattering studies revealed that these excipient matrices undergo high frequency molecular vibrations that cause instability, denaturation and loss of activity.


Aridis’ macromolecular stabilization technology uses small molecular weight, FDA approved stabilizers (called plasticizers) to dynamically suppress high frequency molecular vibrations induced by the drug’s environment. These molecules essentially fill the molecular gaps between the protein surface and the conventional pharmaceutical stabilizers to reduce molecular mobility, consequently promotes long term stability over and beyond what can be achieved with the sugar stabilizers alone*.


Our formulation technology can convert proteins or complex vaccines that require refrigerators or freezers for storage and distribution into ambient temperature (25°C) stable products with shelf life that is measured in years. This formulation mechanism represents a new paradigm in pharmaceutical stabilization that is applicable to a wide variety of drying processes (including lyophilization) and products. These formulation stabilization technologies have been demonstrated in a number of proteins and vaccines including 4 different IgG monoclonal antibodies, several different subunit proteins (anthrax rPA, influenza HA), virus like particles, live virus vaccines (influenza, measles, rotavirus, adenovirus, etc), live bacterial vaccines (Salmonella ty21a, Franciscella LVS, etc.). Further validation has been from >10 different grant funding awards from US government agencies and non-governmental agencies totaling more than $11m.



*Cicerone MT, Tellington A, Trost L, Sokolov A. Substantially improved stability of biological agents in dried form. BioProc. Int. 2003. 1:36–47; and Cicerone MT and Soles CL. Fast dynamics and Stabilization of Proteins: Binary glasses of Trehalose and Glycerol. Biophysical J. 2004. 86:3836-45.

Stabilization of Biopharmaceuticals