33237-32-0

Upstream product

• 3235-15-2 N-benzyloxycarbonyl-L-alanyl-L-phenylalanyl hydrazide 
• 147-85-3 L-proline 
• 1142-20-7 N-Cbz-Ala 
• 3235-14-1 (S)-2-((S)-2-Benzyloxycarbonylamino-propionylamino)-3-phenyl-propionic acid methyl ester 
• 2768-53-8 N-benzyloxycarbonyl-L-alanyl-L-phenylalanine 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 36477-14-2 5-benzyl-10b-methoxy-2-methyl-3,6-dioxo-octahydro-imidazo[1,2-a]pyrrolo[2,1-c]pyrazine-1-carboxylic acid benzyl ester 
• 35802-19-8 5-benzyl-1-benzyloxycarbonyl-10b-hydroxy-2-methyl-1,8,9,10,10a,10b-hexahydroimidazo<1,2-a>pyrrolo<2,1-c>pyrazine-3,6(2H,5H)-dione 
• 35749-06-5 N-benzyloxycarbonyl-L-alanyl-L-phenylalanyl-L-proline p-nitrophenyl ester 

Relevant academic research and scientific papers

Engineered Substrate for Cyclooxygenase-2: A Pentapeptide Isoconformational to Arachidonic Acid for Managing Inflammation

Beyond the conventional mode of working of anti-inflammatory agents through enzyme inhibition, herein, COX-2 was provided with an alternate substrate. A proline-centered pentapeptide isoconformational to arachidonic acid, which exhibited appreciable selectivity for COX-2, overcoming acetic acid- and formalin-induced pain in rats to almost 80%, was treated as a substrate by the enzyme. Remarkably, COX-2 metabolized the pentapeptide into small fragments consisting mainly of di- and tripeptides that ensured the safe breakdown of the peptide under in vivo conditions. The kinetic parameter Kcat/Km for COX-2-mediated metabolism of the peptide (6.3 × 105 M-1 s-1) was quite similar to 9.5 × 105 M-1 s-1 for arachidonic acid. Evidenced by the molecular dynamic studies and the use of Y385F COX-2, it was observed that the breakage of the pentapeptide has probably been taken place through H-bond activation of the peptide bond by the side chains of Y385 and S530.

Structural Studies of Azacyclos derived from Linear Tripeptides

N-Benzyloxycarbonyl-L-alanyl-L-phenylalanyl-L-proline p-nitrophenyl ester (4) and its N-p-bromobenzyloxycarbonyl analogue (2) each cyclize in alkaline aqueous medium to give a tricyclic system containing a free hydroxy-group derived from intramolecular addition of NH to amide carbonyl.Both the five-membered rings of the tricyclic system assume an envelope conformation.In the six-membered ring only the carbon atom bearing the cyclolic hydroxy-group is out of the plane of the other ring atoms.The benzylic side-chain of the phenylalanine residue adopts an extended conformation in both azacyclols.The crystal and molecular structures and spectral data for the tricyclic compounds (3) and (5) are reported.