Understanding the rules and distinguishing the differences between normal and aberrant protein aggregation is key to answering elemental questions from why we age? to what triggers the early onset of neurodegenerative diseases? In this project we focus on resolving the aggregation pathways and aggregated states of proteins implicated in the pathology of Alzheimer's disease using scanning probe microscopy and chemical spectroscopy.

To this end, we characterise protein aggregates such as amyloid beta and tau isoforms at buffered aqueous solution-solid interfaces and use this information as guidelines to classify protein aggregates in body fluids (blood and cerebrospinal fluid) from individuals at various stages of decline in memory and cognition.