Abstract
A facile automated solid phase method for the synthesis of internally quenched, fluorogenic protease substrates is described. Substrates specifically tailored to represent putative cleavage sites for the normal secretory processing pathway and the amyloidogenic processing pathway(s) of the Alzheimer's disease amyloid precursor protein (APP) have been prepared by this method, and utilized to identify neural protease activities in normal and Alzheimer's disease brain tissue.
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