123482-69-9

Upstream product

• 18162-48-6 tert-butyldimethylsilyl chloride 
• 154160-25-5 (2R,4S,5S)-5-tert-Butoxycarbonylamino-4-hydroxy-2-methyl-6-phenyl-hexanoic acid 
• 104293-55-2 [1-((2S,4R)-4-Methyl-5-oxo-tetrahydro-furan-2-yl)-2-phenyl-ethyl]-carbamic acid tert-butyl ester 
• 193338-94-2 (5S,1'S)-carbetoxy-5-<1-<<(1',1-dimethylothoxy)carbonyl>amino>-2-phenylmethyl>dihydrofuran-2(3H)-one 
• 133333-27-4 tert-butyl (1S)-1-[(2S)-5-oxotetrahydrofuran-2-yl]-2-phenylethylcarbamate 

Downstream Products

• 123482-65-5 [(1S,2S,4R)-1-Benzyl-4-((1S,2S)-1-cyclohexylmethyl-2-hydroxy-4-isobutylcarbamoyl-pent-4-enylcarbamoyl)-2-hydroxy-pentyl]-carbamic acid tert-butyl ester 

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.

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.

Renin inhibitors based on dipeptide analogues. Incorporation of the hydroxyethylene isostere at the P2/P3 sites

The synthesis of a series of renin inhibitors in which the P2 and P3 amino acids are replaced with the hydroxyethylene dipeptide isostere is reported. In vitro evaluation of the inhibitors has revealed that this isostere is an accept