Chang, Howard
Howard is a third year trainee and is in the Department of Chemistry and Biochemistry. His research mentor is Dr. David Eisenberg. He received a B.S. degree in 2007 from UC San Diego.
Mentor: Dr. David Eisenberg
More than 20 human diseases are found to be associated with ordered protein aggregates. These amyloid-associated diseases, including amyotrophic lateral sclerosis (ALS), Alzheimer's disease, and Parkinson's disease, affect thousands in the United States, causing a variety of organs to malfunction. Recent milestones in structural and computational biology allow us to now attack amyloidoses on an atomic level. To this end, we have adapted the Rosetta Design algorithm to design tight-packing inhibitors of amyloid formation. We have already demonstrated that this approach is effective in vitro, for the tau protein associated with Alzheimer's disease. I intend to continue developing this tau fibrillation inhibitor for therapeutic purposes. In doing so, I seek to also advance our understanding of Alzheimer's disease; specifically inhibiting fibril formation will help elucidate the role of fibrils in the cytotoxicity of this and other protein aggregation diseases. With success, another objective is to create a general framework for transitioning from a computationally-designed, tight packing peptide to a rational drug for amyloid diseases.
