INOR 617 |
| Transmissible spongiform encephalopathies (TSE's) or proin diseases (e.g. scapie (a disease of sheep, Kuru, Creutzfeldt-Jakob Disease (CJD), Gerstmann-Strau?ler-Scheinker, fatal familial insomnia (in humans) and Bovine Spongiform Encephalopathy (BSE or mad cow disease) are fatal neurological disorders thought to be cause by the misfolding of the neuronal membrane prion protein (PrP). A conformation change of normally folded PrP (PrPC) to mis-folded scapie form (PrPSc) occurs through an unidentified mechanism, though generally believed to be induced by the exposure of PrPC to PrPSc. The widespread occurrence of PrP's in animal has created much public awareness especially because of the bovine spongiform encephalopathy (BSE) in cattle because it has been speculated that the ingestion of BSE tainted meat will induce a prion disease in humans. It has been demonstrated that transition metal ions such as CuII and NiII can coordinate to a segment of the prion protein, which induce the PrPc to PrPSc transformation. To better understand the role of transition metal coordination to the neurotoxic PrP segment, we have prepared several metal adducts of this fragment using solid phase peptide synthesis (SPPS) techniques. The physical and structural properties of these metallopeptides have been characterized using UV/Vis, CD, EPR, electrochemistry and XAS. These studies suggest the roles PrP transition metal adducts play in promoting prion diseases. |
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Inorganic Modeling of Biological Systems
7:00 PM-10:00 PM, Tuesday, August 21, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Inorganic Chemistry |