(5aq) Molecular Recognition in Bioprocessing, Biosensing and Disease Researchmolecular Recognition in Bioprocessing, Biosensing and Disease Research

Many different biological processes involve the interaction of proteins with other proteins or small chemical molecules, including enzymatic reactions, viral entry into cells, and cell-to-cell signaling. These molecular recognition events are the bases for life as we know it, yet they are not well understood. The chemical engineer is ideally suited to study a plethora of these protein interactions and apply them to many different challenges. Some of these challenges include improving the sustainability of biological purification processes by creating new affinity resins for more efficient purification and virus removal steps. Molecular recognition could also be used to create surfaces that could function as a biosensor for environmental and human toxins. The continued study of protein-protein interactions could also reveal the mechanism of cell destruction in many diseases, leading to improved treatments and possibly cures to these diseases. All of these challenges can be met by studying the biophysical interaction of proteins with other entities at a molecular level. This can be accomplished with a focus on thermodynamics and kinetics, both of which are traditional chemical engineering areas. I have experience in different aspects of molecular recognition. I have worked on the discovery of small peptide ligands that bind to porcine parvovirus (PPV) a small nonenveloped virus. The peptides were discovered from the screening of a solid-phase combinatorial library. Many trimeric peptides were discovered that completely remove PPV when it is spiked into saline. One trimer, WRW, has been found that can clear PPV from the first three column volumes from a solution of 7.5% human blood plasma spiked with PPV. These peptide columns were compared to a weak ion exchange resin that was able to clear considerably less PPV from the same spiked solutions. This peptide ligand has the ability to specifically bind to the target virus. This molecular recognition can be used for removal, detection, and concentration of virus solutions. I would like to continue my work by discovering new and interesting molecular recognition surfaces and probing their specificity. I have also worked on the aggregation of amyloid proteins and their implications to human diseases. The aggregation of amyloid proteins can be manipulated to change the rate of aggregation formation, the morphology of the aggregate formed, and the toxicity of the aggregates. By adding different osmolytes to solutions of the amyloid peptide Aβ, we have been able to discover different morphological changes in the aggregates formed with little change to the rate of aggregate formation. This will continued to be probed to examine the toxicity and stability of these aggregates. All of this research involves the molecular recognition of proteins and peptides. I plan to continue my research career in this area to improve bioprocessing, create biosensors, and to probe the mechanisms of human diseases.