Protein aggregation plays a huge role in developing new biomaterials and understanding the mechanisms responsible for a number of neurodegenerative diseases, including Alzheimer’s disease. The rate at which proteins aggregate and the way in which they aggregate is dependent on a variety of factors. Variations in conditions such as temperature, pH, protein concentration and the addition of metal ions such as zinc can affect whether the protein will form fibrils or particulates and how fast the aggregates will form. By understanding the mechanisms driving protein aggregation we can begin to investigate new techniques and drug systems for dealing with neurodegenerative disease as well as creating functional biomaterials using proteins. Here we present results gathered using light scattering spectroscopy and infrared analysis for several proteins where the conditions have been altered to either promote the formation of fibrils or particulate aggregates. This research will eventually give us important information about how to control protein aggregation and modify the mechanisms to produce an array of beneficial products including drugs and biological materials.