Abstrakt
Neuritic plaques, which are situated in the brain of Alzheimer's disease (AD) patients, are composed mainly of peptides containing 40 or 42 amino acid residues known as ßamyloid plaques (Aß). The Aß peptide is the result of the enzymatic cleavage of the amyloid precursor protein (APP).
In the so-called amyloidogenic pathway, the ßsecretase enzyme releases a protein fragment (C99), which is subsequently metabolized by the enzyme γ-secretase. Monomer forms of Aß are turned into oligomer forms, which are the main cause of cellular neuronal death in AD patients.
The following study is focused on γ-secretase inhibitors that can slow down the production or accumulation of pathologic Aß deposits. γ-Secretase inhibitors that reached different phases of clinical trials are particularly reported as well as other promising groups of these analogues