28426-51-9

Basic information

• Product Name: L-Proline, 1-[N-[(phenylmethoxy)carbonyl]-L-phenylalanyl]-, methyl ester
• CAS NO: 28426-51-9
• Molecular Formula: C23H26N2O5
• Molecular Weight: 410.47
• Mol File: 28426-51-9.mol
• Article Data: 12

Chemical Properties

• CAS DataBase Reference: L-Proline, 1-[N-[(phenylmethoxy)carbonyl]-L-phenylalanyl]-, methyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: L-Proline, 1-[N-[(phenylmethoxy)carbonyl]-L-phenylalanyl]-, methyl ester(28426-51-9)
• EPA Substance Registry System: L-Proline, 1-[N-[(phenylmethoxy)carbonyl]-L-phenylalanyl]-, methyl ester(28426-51-9)

Safety Data

• Hazardous Substances Data: 28426-51-9(Hazardous Substances Data)

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 2577-48-2 methyl (2S)-pyrrolidine carboxylate 
• 2578-84-9 N-benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester 
• 52641-32-4 N-benzyloxycarbonyl-L-phenylalanyl chloride 
• 2133-40-6 L-proline methyl ester monohydrochloride 
• 87072-42-2 Z-L-phenylalanine DCHA salt 
• 41518-17-6 Z-Phe-O-COO-isoBu 
• 63-91-2 L-phenylalanine 
• 501-53-1 benzyl chloroformate 
• 3588-57-6 Z-DL-Phe-OH 
• 175446-63-6 proline acid chloride 
• 147-85-3 L-proline 

Downstream Products

• 184295-92-9 (2S,3R)-2-{[(S)-1-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionyl)-pyrrolidine-2-carbonyl]-amino}-3-hydroxy-butyric acid methyl ester 
• 184295-93-0 (2S,3S)-2-{[(S)-1-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionyl)-pyrrolidine-2-carbonyl]-amino}-3-hydroxy-butyric acid methyl ester 
• 184296-04-6 Cbz-Val-Ser(TBDMS)-D-Phe-Ser(TBDMS)-Phe-Pro-allo-Thr-OMe 
• 184295-97-4 Cbz-D-Val-Ser(TBDMS)-D-Phe-Ser(TBDMS)-Phe-Pro-allo-Thr-OMe 
• 184296-05-7 Cbz-Val-Ser(TBDMS)-D-Phe-Ser(TBDMS)-Phe-Pro-allo-Thr(oxaz)-OMe 
• 184295-98-5 Cbz-D-Val-Ser(TBDMS)-D-Phe-Ser(TBDMS)-Phe-Pro-allo-Thr(oxaz)-OMe 
• 184296-07-9 (5S,8S,11R,14S,17R,20S,22aS)-5,11-Dibenzyl-8,14-bis-(tert-butyl-dimethyl-silanyloxymethyl)-20-((S)-1-hydroxy-ethyl)-17-isopropyl-hexadecahydro-3a,6,9,12,15,18,21-heptaaza-cyclopentacyclohenicosene-4,7,10,13,16,19,22-heptaone 
• 184296-10-4 (5S,8S,11R,14S,17S,20S,22aS)-5,11-Dibenzyl-8,14-bis-(tert-butyl-dimethyl-silanyloxymethyl)-20-((S)-1-hydroxy-ethyl)-17-isopropyl-hexadecahydro-3a,6,9,12,15,18,21-heptaaza-cyclopentacyclohenicosene-4,7,10,13,16,19,22-heptaone 
• 184296-14-8 (2S,8S,11S,14R,17S,20S,23S,24R)-8,14-Dibenzyl-11,17-bis-hydroxymethyl-20-isopropyl-24-methyl-25-oxa-6,9,12,15,18,21,26-heptaaza-tricyclo[21.2.1.0^2,6]hexacos-1⁽²⁶⁾-ene-7,10,13,16,19,22-hexaone 

Relevant articles and documents

Total synthesis of wewakazole B

Wewakazole B is a novel cyclodecapeptide with highly potent cytotoxic activity isolated from a sample of M. producens collected from the Red Sea. It contains nine common and three modified amino acid residues. The first total synthesis of Wewakazole B was successfully achieved on a gram scale, unambiguously confirming its structure. Notable features include the careful choice of amino acid-protecting groups and the construction of three different substituted oxazoles present in this natural product.

Dynamic combinatorial libraries of hydrazone-linked pseudo-peptides: Dependence of diversity on building block structure and chirality

Expanding on our earlier building block architecture [(MeO) 2CH-Linker-Pro-X-NHNH2 where X = Phe, Cha], we have produced a series of new pseudo-dipeptides [(MeO)2CH-Linker-Pro-X- NHNH2 where X = Val, Leu, Ile, A

Relationship between the hydrophobicity of dipeptides and the Michaelis-Menten constant Km of their hydrolysis by carboxypeptidase-Y and carboxypeptidase-A

The enzymatic hydrolysis of dipeptides by carboxypeptidase-Y and carboxypeptidase-A was investigated. In the enzymatic hydrolysis of the dipeptides, a good linear relationship (r = 0.997 and 0.999) was found between the Michaelis-Menten constant (Km) and the hydrophobicity of the substrates evaluated from relative elution volume in reversed-phase HPLC. The correlation suggests that the hydrophobicity of the C-terminal amino acid is a major factor in governing the stability of the enzyme-substrate complex. The difference in the slope of the linear-regression lines seems to reflect the degree of relative hydrophobicity of the binding pockets in carboxypeptidase-Y and carboxypeptidase-A.