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Prana Biotechnology Presents New Key Findings on PBT2

ker protein synaptophysin.

The amyloid plaques which are the main pathological feature of the brains of Alzheimer's sufferers are composed of aggregates of the Abeta protein. The Alzheimer's research community largely supports the hypothesis that small, soluble, mobile aggregates (oligomers) of the Abeta protein are the cause of neurotoxicity in AD. PBT2's ability to inhibit the generation and toxicity of these oligomers, as well as preventing the hyperphosphorylation of tau, while improving cognition, supports the disease modifying potential of PBT2 and other drugs in the Prana development pipeline.

Geoffrey Kempler, Chairman and Chief Executive Officer of Prana commented: "The results of these studies are encouraging and lend further support to the theories driving development of PBT2. We continue to improve our understanding of PBT2's functionality and potential for disease modification as we move forward with formal clinical development. The ongoing PBT2 Phase IIa trial in early Alzheimer's patients is on track to complete dosing by the end of this year and report early in 2008."

The technique of in vivo brain microdialysis recently adopted as a research tool by Prana scientists provides a unique insight into a dynamic metabolic process, allowing researchers to sample secretions from the brains of conscious, unrestrained test animals freely interacting with their environment. Sampling from the brains of genetically-engineered AD mouse models which have received single or sequential oral doses of PBT2, it was found that the drug exerts its inhibitory effects upon the target molecule, Abeta, rapidly and reproducibly without causing "rebound" effects observed with other drugs in development. Most particularly, a dramatic reduction was observed in soluble oligomers of the size range identified in the literature as the most toxic form of Abeta amyloid in AD.

The findings of these studies confirm and expand upon data presented by the Compan
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