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Biophysical Measurements of Protein-Protein Interactions
Alzheimer's disease (AD) is one of the world's leading causes of death, with the root cause being the brain's degradation and its memory capabilities, eventually causing dementia. Due to AD's sheer prominence, it has become a highly studied disease focusing on the critical protein targets that cause significant changes in the brain. Studying the protein systems can show many ways to fight AD, from new diagnostic targets to understanding upstream causes that may indicate a therapeutic path to AD. This work will study protein systems further using biophysical methods to solicit data on the protein-protein interactions related to AD.
The first biophysical method introduced is fluorescence correlation spectroscopy (FCS), which uses spatiotemporal analysis of low concentration fluorescently tagged proteins' binding affinities. FCS will be used to evaluate the binding of antibody AT270 to phosphorylated Tau peptides to better understand their capabilities as a biomarker for diagnosing AD. The second biophysical method in this work is isothermal calorimetry (ITC), a label-free technique to obtain the binding affinities of proteins through the thermodynamics of binding. ITC will be used on calmodulin, a neuronal protein with multiple downstream binding partners associated with AD. ITC's binding results thus can be an avenue for evaluating the potential of therapeutics or diagnostics using binding partners of calmodulin.