We are interested in problems related to the loss of natural structure of proteins (“misfolding”) as it relates to their use as pharmaceuticals. Experimental, modeling, and simulation approaches are being exploited to elucidate and describe protein structural changes that occur during protein purification. In related research we are investigating the undesirable self-association of proteins (“aggregation”), which is important for biopharmaceutical applications and central to several human neurodegenerative diseases.

In collaboration with the Lander's group in the Chemistry department, microfluidic devices representing a thin slice through a soil matrix are used to directly observe distributions of bacteria labeled with green fluorescent protein (GFP) as they sense and swim toward to sources of chemical pollutants in their surroundings. These devices can also be used to directly observe particle streamlines around single collector surfaces to better design clean bed filtration systems.

Proteins play key roles in the most of processes in living organisms to maintain life. Protein engineering is a powerful tool to generate new proteins or to improve properties of the existing proteins. Such engineered proteins have been widely used to address many challenges in various biomedical fields, including protein-based drug development, gene and drug delivery, and tissue engineering.

Drug resistance is one of the biggest challenges in the pharmacological treatment of infectious diseases, and current informatics based drug discovery methods are not well suited to rapidly develop new drug variants that can successfully overcome resistance.  Our research has demonstrated that statistical mechanical methods can predict ligand binding affinities to within 1 kcal/mol in simple atomistically detailed systems, a level that becomes useful for the pharmaceutical industry.  We are working on making these approaches useful in industrial drug design.