Neurotoxic protein oligomers

Oligomers and fibrils (amyloids) formed from several proteins are associated with a variety of neurodegenerative diseases including Alzheimer's, Parkinson's, Huntington's, and ALS. Unfortunately, for many of the proteins involved in these diseases, the mechanisms responsible for amyloid formation and the structures of various intermediates (e.g. oligomers and protofibrils) along the fibrillization pathway are notoriously difficult to study. This is especially true of oligomeric species, which are difficult to isolate, metastable, and disproportionately toxic relative to higher molecular weight protofibrils and fibrils. The continued study of oligomeric species will require breakthroughs in structural biology as well as an improved understanding of protein homeostasis and fibrilization kinetics. As an interdisciplinary team with a foundation based on Chemical Engineering, we are developing tools that will aid in the isolation of neurotoxic protein oligomers with the ultimate goal of establishing structure-function relationships for these species.


Metal nanoparticles produced from the biological reduction of soluble metal salts show promise as catalysts for processes relevant to water treatment and environmental remediation. In some cases, nanoparticles produced in this manner exhibit superior activity to those synthesized using more traditional methods. However, control over biologically-produced metal nanoparticle size and crystal morphology is still a challenge and varies significantly between organisms. Using tools in synthetic chemistry, surface science, and chemical biology, we are trying to understand the biochemical mechanisms that underly nanoparticle formation and whether these can be manipulated in a rational manner to give materials with improved catalytic properties.