Massachusetts Institute of Technology
Department of Chemical Engineering





Trout Group Member

Dr. Curtiss P. Schneider
Postdoctoral Associate

Department of Chemical Engineering
Massachusetts Institute of Technology
Room: E19-536
77 Massachusetts Ave.
Cambridge, MA 02139 USA

Phone: (617) 253-6585
Fax: (617) 253-2272


B.S. Chemical Engineering from Colorado School of Mines – May, 2004

Ph. D. Chemical Engineering, Massachusetts Institute of Technology - Dec 2010

Research Summary

Stabilizing Proteins Against Aggregation

Proteins in solution have a tendency to aggregate due to favorable free energy for the reduction of solvent-accessible area, particularly of hydrophobic groups. Proteins in the aggregated state generally do not have the same biological activity as proteins in the native state, they can often be immunogenic, and my even have acute toxic effects in vivo. This is an especially grave problem for the pharmaceutical industry, where it is desired to store proteins at the highest possible concentration over long periods of time. Thus it is essential to develop strategies for preventing aggregation to extend the shelf life of therapeutic proteins.

One such strategy is the use of “neutral crowder” additives. In this case, there is the potential for a “gap effect” to arise if the additive is significantly larger than the primary solvent. This effect is analogous to osmotic stress. The large additive will be excluded from solvating the gap between protein molecules for steric reasons, thus increasing the free energy of the protein-protein encounter complex. If the additive does not interact with the isolated protein any differently than water, the primary effect is an increase in the activation energy of the protein association reaction, thus slowing the rate of aggregation.


Last Updated: January 24, 2011