pH induced structural alterations of lysozyme in aqueous sugar solutions

This proposal is related to our previous studies of how the disaccharides trehalose and sucrose affect the structural and dynamical properties of myoglobin. In previous NIMROD experiments we found that both sugars were able to prevent aggregation of myoglobin in an aqueous solution. We also found that the protein was preferentially hydrated by water, and that this effect was strongest for trehalose. In this study we are replacing myoglobin with lysozyme to determine how the sugars affect detrimental pH induced structural alterations of lysozyme and the formation of amyloid fibrils, which is known to cause many neurodegenerative diseases, such as Alzheimer’s. With this study of lysozyme we will also be able to determine whether our previous results are unique for myoglobin, or will be similar for other proteins, as well as if disaccharides can reduce the formation of amyloid fibrils.