154160-25-5

Upstream product

• 104293-55-2 (3R,5S,1'S)-5-<1-<<(tert-butyloxy)carbonyl>amino>-2-phenylethyl>-3-methyldihydrofuran-2(3H)-one 
• 24424-99-5 di-tert-butyl dicarbonate 
• 193338-94-2 (5S,1'S)-carbetoxy-5-<1-<<(1',1-dimethylothoxy)carbonyl>amino>-2-phenylmethyl>dihydrofuran-2(3H)-one 
• 154160-21-1 (2S,3S)-2-Dibenzylamino-5-[1,3]dioxan-2-yl-1-phenyl-pentan-3-ol 
• 154160-19-7 (2S,3S)-2-Dibenzylamino-5-[1,3]dioxolan-2-yl-1-phenyl-pentan-3-ol 
• 154160-17-5 (S)-2-Dibenzylamino-5-[1,3]dioxan-2-yl-1-phenyl-pentan-3-one 
• 154160-16-4 (S)-2-Dibenzylamino-5-[1,3]dioxolan-2-yl-1-phenyl-pentan-3-one 
• 143337-98-8 (5S,1'S)-5-(1'-(dibenzylamino)-2'-phenylethyl)dihydrofuran-2(3H)-one 
• 131150-35-1 (S)-2-(dibenzylamino)-N'-methoxy-N'-methyl-3-phenylpropane amide 
• 95437-43-7 (S)-2-(N,N-dibenzylamino)-3-phenylpropanoic acid 
• 133333-27-4 tert-butyl (1S)-1-[(2S)-5-oxotetrahydrofuran-2-yl]-2-phenylethylcarbamate 

Downstream Products

• 123482-69-9 (2R,4S,5S)-5-tert-butoxycarbonylamino-4-(tert-butyldimethylsilyloxy)-2-methyl-6-phenylhexanoic acid 

Relevant academic research and scientific papers

Structure-based design: Potent inhibitors of human brain memapsin 2 (β-secretase)

Memapsin 2 (β-secretase) is one of two proteases that cleave the β-amyloid precursor protein (APP) to produce the 40-42 residue amyloid-β peptide (Aβ) in the human brain, a key event in the progression of Alzheimer's disease. On the basis of the X-ray crystal structure of our lead inhibitor (2, OM99-2 with eight residues) bound to memapsin, we have reduced the molecular weight and designed potent memapsin inhibitors. Structure-based design and preliminary structure-activity studies have been presented.

Stereoselective Synthesis of a Hydroxyethylene Dipeptide Isostere

A stereoselective synthesis of a hydroxyethylene dipeptide isostere for Phe-Gly, (4S, 5S)-4-hydroxy-5-amino-6-phenylhexanoic acid, is described.The use of dibenzyl protecting groups on ketoamine 5 accounts for the selectivity on reduction.Also, the dibenzyl group plays a role in directing the introduction of a third chiral center.

HIV-1 protease inhibitors based on hydroxyethylene dipeptide isosteres: An investigation into the role of the P1' side chain on structure-activity

A systematic investigation was undertaken to determine the role of the P1' sidechain in a series of hydroxyethylene isostere based inhibitors of HIV-1 protease. Substitution and homologation of the benzyl P1' side chain of the Phe-Phe isostere based pseudo peptides 1 (L-682,679) and 2 (L-685,434) with various heteroalkyl groups leads to a series of extremely potent inhibitors of the enzyme. Several examples of the most potent inhibitors were very effective in an ex vivo cell based viral spread assay using human H9 T- lymphocytes and the IIIb isolate of HIV-1. Compound 19 is 120 times more potent than 1 and 16 times more potent than 2 in inhibiting the spread of infection in this assay.