1399317-86-2

Upstream product

• 72155-45-4 Boc-L-phenylalaninal 
• 1399317-77-1 C₂₄H₄₁N₃O₄ 
• 1399317-73-7 tert-butyl [(2S,3S)-3-hydroxy-1-(isobutylamino)-1-oxohexan-2-yl]carbamate 
• 1399317-69-1 (2S,3S)-ethyl 2-[(tert-butoxycarbonyl)amino]-3-hydroxyhexanoate 
• 1399317-64-6 (2S,3S)-ethyl 2-azido-3-hydroxyhexanoate 
• 1399317-60-2 (2R,3S)-ethyl 3-Hydroxy-2-{[(4-nitrophenyl)sulfonyl]-oxy}hexanoate 
• 108666-29-1 (2R,3S)-ethyl 2,3-dihydroxyhexanoate 
• 27829-72-7 ethyl (E)-hex-2-enoate 
• 1399317-08-8 C₁₆H₂₀N₂O₄S 
• 1399317-04-4 C₁₇H₂₂N₂O₄S 

Relevant academic research and scientific papers

Inhibitors of Memapsin 2 Cleavage for the Treatment of Alzheimer's Disease

Proteases such as memapsin 2 are important enzymes, playing roles in a variety of diseases including Alzheimer's Disease. The inventors have developed inhibitors of memapsin 2 and methods of use therefore in the treatment of disease.

Structure-based design of highly selective β-secretase inhibitors: Synthesis, biological evaluation, and protein-ligand x-ray crystal structure

The structure-based design, synthesis, and X-ray structure of protein-ligand complexes of exceptionally potent and selective β-secretase inhibitors are described. The inhibitors are designed specifically to interact with S1′ active site residues to provide selectivity over memapsin 1 and cathepsin D. Inhibitor 5 has exhibited exceedingly potent inhibitory activity (Ki = 17 pM) and high selectivity over BACE 2 (>7000-fold) and cathepsin D (>250000-fold). A protein-ligand crystal structure revealed important molecular insight into these selectivities. These interactions may serve as an important guide to design selectivity over the physiologically important aspartic acid proteases.