UC Santa Barbara

Protein aggregation has long been a topic of interest within the scientific community due to its connection to various neurodegenerative disorders such as Alzheimer’s Disease and Parkinson’s Disease. While amyloidogenic fibrils were long thought to be the primary toxic species involved in these disorders, in recent years it has been shown that smaller, intermediary oligomers are more toxic than the mature fibrils. This has prompted additional study into these intermediary oligomers, and subsequently the potential aggregating behaviors of small metabolites such as nucleobases and individual amino acids. In this dissertation I will focus on the aggregation of select amino acids, and examine the effects of various alkali metal cations on the oligomer formation pathway and their potential role in stabilizing and promoting these aggregates. This has been done through a combination of experimental and computational techniques, namely ion mobility mass spectrometry and molecular dynamics.