Today, Prana Biotechnology Ltd. announced that its lead drug candidate for Parkinson's disease and movement disorders, PBT434, will be presented at two international conferences this month, reporting the key finding that PBT434 reduces the aggregation and accumulation of a key protein (alpha-synuclein) in multiple transgenic animal models of Parkinson's disease.
The alpha-synuclein (s.n.) protein aggregates inside the nerve cells of the substantia nigra, which is the part of the brain responsible for controlling movement and the part of the brain that is progressively damaged in Parkinson's disease. The (s.n.) protein aggregates are linked with the onset and progression of Parkinson's disease, and PBT434 significantly prevented the death of substantia nigra brain cells in three different Parkinson's disease animal models.
"A treatment for Parkinson's disease and other movement diseases that actually modifies the course of the diseases remains a major unmet medical need," said Robert Cherny, an associate professor and the head of research for Prana. "Our data suggests that PBT434 intervenes in metal dependent pathways which otherwise promote the aggregation of alpha-synuclein. Thus, PBT434 prevents the death of substantia nigra cells. We have observed marked improvements in motor function and coordination with PBT434."
Presenting the new data at the 11th International Basal Ganglia Society Meeting - March 3-7 in Eilat, Israel - will be Associate Professor David Finkelstein. He will present a talked entitled "PD: Towards New Disease Modifying Therapies."
Additionally, Associate Professor Kevin Barnham will discuss PBT434 at the 11th International Conference on Alzheimer's and Parkinson's disease, March 6-10 in Florence, Italy. His presentation will be entitled "The Role of Nitrated Tau in PD."
Prana is developing PBT434 with support from the Michael J. Fox Foundation for Parkinson's Disease Research.
For more information about Prana Biotechnology, visit www.pranabio.com
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