I completed an integrated Master’s degree in Natural Sciences at the University of Leeds, where I majored in chemistry. After studying a broad range of modules across chemistry, biochemistry and mathematics, I begun to develop a particular interest in chemical biology and medicinal chemistry. My degree allowed me to experience interdisciplinary research early on and I completed a chemical biology Master’s research project, where I investigated protein-protein interactions using cross-linkers. Following this, I knew that I wanted to continue working in this field, which I am able to do at Leeds, where I will be investigating the aggregation of proteins in amyloid diseases.
A multitude of diseases are classified as amyloid diseases, including Parkinson’s disease and dialysis-related amyloidosis. Amyloid diseases can involve both intrinsically disordered proteins or globular proteins and involve protein misfolding and aggregation. This PhD project exploits chemical biology approaches to understand and manipulate the aggregation behaviour of proteins which form amyloid fibrils in disease. It involves synthesising small molecule modulators of protein aggregation and identifying the site at which they bind to the protein of interest using analytical techniques, including kinetic assays, binding assays and structural analysis using NMR and X-ray crystallography.