Using a set of simple experiments that control the amount and character of interface present, the Talaga Lab was able to establish that the in vitro aggregation behavior of the protein α-synuclein is dominated by reactions at interfaces. In the absence of nucleating oligomers, the protein does not aggregate unless highly hydrophobic interfaces are present. Currently the Talaga Lab is chemically modifying quartz and mica surfaces and glass mixing balls to obtain controlled hydrophobicity at the interfaces for aggregation studies.