CHARACTERIZATION OF INTERMEDIATES IN AMYLOID FIBRIL FORMATION

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The overall goal of our research is to determine the molecular basis for protein aggregation, especially in the context of protein deposition diseases. This proposal is to characterize early intermediates in the process of amyloid fibril and amorphous aggregate formation. Preliminary investigations suggest the presence of soluble oligomeric intermediate species. SAXS will be used to characterize both the precursor partially-folded intermediates and early oligomeric intermediates in aggregation, as a function of experimental conditions, especially those correlating with increased rates of aggregation. The proteins to be studied (IgG light chains, alpha-synuclein, tau, leptin and insulin) are all associated with important diseases.