Transmissible spongiform encephalopathies (TSE's) or proin diseases are fatal neurological disorders thought to be caused by the mis-folding of the neuronal membrane prion protein (PrP). A conformation change of normally folded PrP (PrPC) to mis-folded PrPSc) through an unidentified mechanism is 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 peptide role of transition metal coordination we have prepared several metal adducts of this PrP fragment. The physical and structural properties of these fragments will be discussed along with the potential physiological roles PrP transition metals adducts might play.