The aggregation of proteins into amyloid fibrils is implicated in numerous chronic diseases affecting millions of people worldwide. These illnesses include Alzheimer’s disease, Parkinson’s disease, and type II diabetes. It is now understood that early-stage aggregates are toxic, prompting a shift from studying mature fibrils to investigating mechanisms of nascent fibril formation and related intermediates. However, there are still challenges in identifying aggregation pathways and detecting early-stage aggregates. My research addresses these challenges on two fronts: (1) investigating the mechanism behind early-stage amyloid aggregates using molecular simulations, specifically with molecular dynamics and the string method sampling technique, and (2) detecting early-stage amyloid aggregates with liquid crystals.
Ashley is from Cary, NC. In 2014, she graduated from Caltech with a B.S. in Chemical Engineering. She then joined the inaugural class of PhD students in the Institute for Molecular Engineering (now the Pritzker School of Molecular Engineering) at the University of Chicago. Ashley is now a graduate student in Prof. Juan de Pablo's group, working on molecular simulations of protein aggregation and liquid crystal sensing applications. In addition to research, Ashley enjoys biking, learning foreign languages, and pushing the limits of apartment gardening.
- Extracting collective motions underlying nucleosome dynamics via nonlinear manifold learning
- Early-stage human islet amyloid polypeptide aggregation: Mechanisms behind dimer formation
- Adaptive enhanced sampling by force-biasing using neural networks
- Human Islet Amyloid Polypeptide: Identifying Early-Stage Aggregation Mechanisms through Molecular Simulation