84120-87-6

Upstream product

• 67-56-1 methanol 
• 17350-84-4 (R)-2-amino-2-methyl-3-phenylpropanoic acid 
• 100-39-0 benzyl bromide 
• 1037074-43-3 (-)-(2S,4R)-3-benzoyl-4-benzyl-4-methyl-2-phenyl-1,3-oxazolidin-5-one 
• 169566-66-9 N²-<(R)-N²-benzoyl-2-methyl-phenylalanyl>-(S)-phenylalanine cyclohexylamide 
• 169738-76-5 (R)-methyl 2-benzamido-2-methyl-3-phenylpropanoate 

Downstream Products

• 285130-54-3 (R)-methyl hippuryl-α-methylphenylalaninate 
• 1429340-60-2 C₂₂H₃₂N₂O₅ 
• 561044-87-9 (-)-(3S,6R,9S,14aR)-6,9-dibenzyl-3-[(R)-7-hydroxy-6-oxooctyl]-6-methyldecahydropyrrolo[1,2-a][1,4,7,10]tetraazacyclododecine-1,4,7,10-tetraone 
• 1429340-64-6 C₃₉H₅₄N₄O₇ 
• 1429340-67-9 (-)-(3S,6R,9S,14aR)-6,9-dibenzyl-3-(but-3-enyl)-6-methyldecahydropyrrolo[1,2-a][1,4,7,10]tetraazacyclododecine-1,4,7,10-tetraone 
• 1445578-67-5 C₄₃H₆₂N₄O₇S₂Si 
• 1445578-66-4 C₄₀H₅₈N₄O₆Si 
• 285130-55-4 (R)-Hippuryl-alpha-methylphenylalanine 
• 325462-13-3 ((CH₃)(CH₂C₆H₅)C₃NO(O))2C(CH₃)2 

Relevant academic research and scientific papers

Flexible synthesis and evaluation of diverse anti-apicomplexa cyclic peptides

A modular approach to synthesize anti-Apicomplexa parasite inhibitors was developed that takes advantage of a pluripotent cyclic tetrapeptide scaffold capable of adjusting appendage and skeletal diversities in only a few steps (one to three steps). The diversification processes make use of selective radical coupling reactions and involve a new example of a reductive carbon-nitrogen cleavage reaction with SmI2. The resulting bioactive cyclic peptides have revealed new insights into structural factors that govern selectivity between Apicomplexa parasites such as Toxoplasma and Plasmodium and human cells.

Hippuryl-α-methylphenylalanine and hippuryl-α-methylphenyllactic acid as substrates for carboxypeptidase A. Syntheses, kinetic evaluation and mechanistic implication

(R)- and (S)-Hippuryl-α-methylphenylalanine [(R)- and (S)-Hipp-α- MePhe] and (S)-hippuryl-α-methylphenyllactic acid [(S)-Hipp-α-MeOPhe] were synthesized and evaluated as substrates for carboxypeptidase A (CPA) in an effort to shed further light on the catalytic mechanism of the enzyme. The rate of CPA-catalyzed hydrolysis of (S)-Hipp-α-MePhe was reduced by 105-fold compared with that of (S)-Hipp-Phe, but the hydrolysis rate of (S)-Hipp-OPhe was lowered by only 6.8-fold by the introduction of a methyl group at the α- position. (R)-Hipp-α-MePhe failed to be hydrolyzed initially, then started to undergo hydrolysis in about 2 h at a much reduced rate. The results of present study may be envisioned on the basis of the proposition that while peptide substrate is hydrolyzed via a tetrahedral transition state formed by the attack of the zinc-bound water molecule at the peptide carbonyl carbon, ester hydrolysis takes the path that involves an anhydride intermediate generated by the attack of the carboxylate of Glu-270 at the ester carbonyl carbon. (C) 2000 Elsevier Science Ltd.