110769-86-3

Upstream product

• 180322-77-4 (1S,2S)-(E)-1-carboxy-1-(methoxycarbonyl)-2-phenylcyclopropane 
• 1036637-32-7 methyl (1S,2R)-1-nitro-2-phenylcyclopropanecarboxylate 
• 100-42-5 styrene 
• 1095278-82-2 methyl (1S,2S)-1-nitro-2-phenylcyclopropanecarboxylate 
• 110769-87-4 C₁₁H₁₃NO₂*C₁₈H₁₄O₈ 
• 100-52-7 benzaldehyde 
• 82112-04-7 Cyclopropyl-Z-phenylalanine methyl ester hydrochloride 
• 3092-20-4 diethyl 2-phenylcyclopropane-1,1-dicarboxylate 
• 5292-53-5 diethyl benzalmalonate 
• 70315-54-7 methyl 1-benzamido-2-phenyl-cyclopropanecarboxylate 
• 150351-79-4 (1S,3S,6S)-6-Isopropyl-5-methoxy-1-phenyl-4,7-diaza-spiro[2.5]oct-4-en-8-one 
• 150351-77-2 (Z,S)-1-Acetyl-3-benzylidene-6-(1-methylethyl)piperazine-2,5-dione 

Downstream Products

• 1191903-14-6 C₂₃H₂₈N₂O₅S 
• 1374241-55-0 C₁₈H₁₇NO₃ 
• 180322-79-6 (1S,2S)-(Z)-1-[N-[[(1,1-dimethylethyl)oxy]carbonyl]amino]-2-phenylcyclopropane-1-carboxylic acid 
• 180322-78-5 (1S,2S)-1-tert-Butoxycarbonylamino-2-phenyl-cyclopropanecarboxylic acid methyl ester 
• 150351-75-0 (1S,2S)-1-[(R)-2-(Adamantan-2-yloxycarbonylamino)-3-(1H-indol-3-yl)-2-methyl-propionylamino]-2-phenyl-cyclopropanecarboxylic acid methyl ester 

Relevant academic research and scientific papers

A formyl peptide substituted with a conformationally constrained phenylalanine residue evokes a selective immune response in human neutrophils

Formyl-Met-Leu-Phe-OH (fMLP) binds to formyl peptide receptors, FPR1 and FPR2, and evokes migration and superoxide anion production in human neutrophils. To obtain a more effective and selective ligand, fMLP analogs in which the Phe residue was substitute

Catalytic asymmetric synthesis of nitrocyclopropane carboxylates

A Cu(I)-catalyzed asymmetric cyclopropanation of alkenes with an iodonium ylide has been developed. The copper source, hypervalent iodine source, solvent, and additives all have a significant effect on the yields and enantioselectivities. High enantioselectivity (up to 99:1 er) and diastereoselectivity (95:5 dr trans/cis) were achieved for a wide range of alkenes. Conditions were developed to convert the trans products to the cis isomers. In addition, 1-nitrocyclopropyl carboxylates were transformed into the corresponding substituted cyclopropane amino acids and aminocyclopropanes. Moreover, a comparative study between Zn- and In-mediated reduction reactions of the nitro group in these compounds with regards to the er erosion in the process is also documented.

Design and synthesis of dipeptidyl nitriles as potent, selective, and reversible inhibitors of cathepsin C

A series of dipeptide nitriles with a thienyl alanine in P2 were identified as potent and selective cathepsin C inhibitors. Incorporation of a substituted cyclopropyl moiety in P1 effectively protects these derivatives against hydrolase activity in whole blood.

PEPTIDYL NITRILES AND USE THEREOF AS DIPEPTIDYL PEPTIDASE I INHIBITORS

The present invention provides compounds of formula (I) in which n, y, X1, X2, A, B, R1, R2, R3, R4 and R5 are as defined in the specification, a process for their preparation, pharmaceutical compositions containing them and their use as dipeptidyl peptidase I (DPPI) inhibitors.

Asymmetric cyclopropanations by rhodium(II) N-(arylsulfonyl)prolinate catalyzed decomposition of vinyldiazomethanes in the presence of alkenes. Practical enantioselective synthesis of the four stereoisomers of 2-phenylcyclopropan-1-amino acid

The rhodium N-(arylsulfonyl)prolinate catalyzed decomposition of vinyldiazomethanes in the presence of alkenes leads to a very general method for the synthesis of functionalized cyclopropanes in a highly diastereoselective and enantioselective mode. A det

Preparation of dipeptoid mimetics for the tetrapeptide cholecystokinin, CCK(30-33)

The diastereoselective synthesis of 2,3-methanophenylalanine methyl esters (5) has been achieved in 58% yield. The preparation of the dehydropeptides (1, R = Me; 2, R = H) and the cyclopropylpeptides (3, R = Me; 4, R = H) possessing good binding affinities for the CCK-A and CCK-B receptors is described. Conformational studies of the dipeptide esters 1 and 3 indicated the presence of a β-turn within the peptide backbone, although there was no preference in type. The Phe and Trp moieties, however, did prefer to be situated on the same side of the peptide turn which is favourable for receptor binding.