Novel Approach to Treat Alzheimer's and Other Diseases Offered by Targeting Cell Memb...( JADO Technologies' Scientists and C...)

JADO Technologies' Scientists and Collaborators Publish Study in Science

DRESDEN, Germany, April 25 /PRNewswire/ -- JADO Technologies GmbH, the leading developer of RAFT intervention therapeutics, announced today the publication of a paper in Science demonstrating a potential novel strategy for therapeutic intervention in Alzheimer's and other diseases by targeting discrete sub-compartments in the cell membrane (RAFTS). The study conducted by JADO scientists together with several academic collaborators will appear in the April 25, 2008 issue of the magazine.

Entitled "Efficient inhibition of the Alzheimer's disease Beta-secretase by membrane targeting", the paper describes how Beta-secretase, the rate-limiting enzyme in the production of Alzheimer's disease associated Beta-amyloid peptide, can be inhibited effectively using compounds anchored to cell membrane RAFTS. Unlike existing approaches for Beta-secretase inhibition that do not account for the intracellular location of the target protein or the different conformation that the protein may assume in this context, these RAFT inhibitors are delivered to the exact site where Beta-secretase executes its neurotoxic activity.

"Our data provide proof-of principle of a new approach for directing small molecule inhibitors to disease causing RAFT targets in cellular membranes. In this instance, by directing inhibition to the sub-compartment where the enzyme is active, the approach has potential to be used in the design of more effective Beta-secretase inhibitors for the treatment of Alzheimer's disease," noted Professor Kai Simons, Max-Planck Institute of Molecular Cell Biology and Genetics and co-founder of JADO. "We believe that this novel strategy can be used to design therapeutics against other RAFT targets in a range of other diseases."

Beta-secretase is internalized from the cell membrane into intracellular compartments (endosomes) where it cleaves its substrate, Amyloid Precursor Pr
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