Boris Schmidt, Stefanie Baumann, Hannes A. Braun and Gregor Larbig Pages 377 - 392 ( 16 )
Most gene mutations associated with Alzheimers disease point to the metabolism of amyloid precursor protein as potential cause. The β- and γ-secretases are two executioners of amyloid precursor protein processing resulting in amyloid β. Significant progress has been made in the selective inhibition of both proteases, regardless of structural information for γ-secretase. Several peptidic and non-peptidic leads were identified and first drug candidates are in clinical trials. This review focuses on the developments since 2003.
Alzheimer's disease, secretase, aspartic protease, inhibitor, presenilin
Clemens Schopf-Institute forOrganic Chemistry and Biochemistry, TU Darmstadt, Petersenstrasse 22, D-64287 Darmstadt, Germany.