This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. From the Raleigh web site: """"""""In certain diseases normally soluble proteins aggregate to form a dense structure called the amyloid fibril. Amyloid deposits are present in individuals suffering from type-II diabetes, Alzheimer's disease and in patients undergoing kidney dialysis. Little is known about the molecular mechanism of amyloid formation. We are studying amyloid formation by the polypeptides amylin and calcitonin. Amylinis a 37 residue peptide which forms amyloid deposits in type-II diabetes while calcitonin forms amyloid deposits in the thyroid. Our work involves the preparation of the peptides via solid phase peptide synthesis, the characterization of the structure of these molecules and studies of the kinetics of amyloid formation."""""""" We are using native MS to determine what multimeric stoichiometries of an Amylin peptide are present as a function of time. Coupling this information to kinetic and toxicity data obtained by the Raleigh lab should provide valuable insights regarding which mer sizes are responsible for the toxic properties of Amylin aggregation.
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