13122-87-7

Basic information

• Product Name: Cbz-Phe-D-Phe-OMe
• Synonyms: Cbz-Phe-D-Phe-OMe
• CAS NO: 13122-87-7
• Molecular Weight: 460.53
• Mol File: 13122-87-7.mol
• Article Data: 8

Chemical Properties

• CAS DataBase Reference: Cbz-Phe-D-Phe-OMe(CAS DataBase Reference)
• NIST Chemistry Reference: Cbz-Phe-D-Phe-OMe(13122-87-7)
• EPA Substance Registry System: Cbz-Phe-D-Phe-OMe(13122-87-7)

Safety Data

• Hazardous Substances Data: 13122-87-7(Hazardous Substances Data)

Upstream product

• 96452-48-1 benzyl pyridin-2-yl carbonate 
• 501-53-1 benzyl chloroformate 
• 1161-13-3 N-Cbz-L-Phe 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 96452-61-8 N-(Benzyloxycarbonyl)-L-phenylalanin-2-pyridylester 
• 117999-37-8 Z-ΔPhe-(S)-Phe-OMe 
• 1059596-58-5 N-Cbz-L-phenylalanine p-tolylthiol ester 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 
• 13033-84-6 D-phenylalanine methyl ester hydrochloride 
• 15028-44-1 DL-phenylalanine methyl ester 
• 21685-51-8 D-phenylalanine methyl ester 

Downstream Products

• 1323358-01-5 C₂₅H₂₆N₆O₅ 
• 80546-83-4 L-phenylalanyl-D-phenylalanine methyl ester 

Relevant articles and documents

Facile Synthesis of Cyclic Dipeptides and Detection of Racemization

Several cyclic dipeptides were synthesized by refluxing methanolic solution of dipeptide methyl esters in high yield and purity.Cyclic dipeptides prepared by the Fischer method, the Nitecki method, and the present methanol-reflux method were compared with

HMDO-promoted peptide and protein synthesis in ionic liquids

Hexamethyldisiloxane (HMDO) has been developed to efficiently promote the metal-free direct coupling of an amino function of one cysteine-free peptide or protein and a C-terminal thioester of the second peptide in ionic liquids. The amide-coupling reaction proceeds smoothly under mild conditions to afford the corresponding products in good to excellent yields (63-94%). Peptide couplings were also achieved using in-situ-generated thioesters by the thioesterification of oxo esters.

α-Chymotrypsin-catalyzed peptide synthesis in frozen aqueous solution using N-protected amino acid carbamoylmethyl esters as acyl donors

A kinetically controlled peptide synthesis catalyzed by α-chymotrypsin was performed in frozen aqueous solution (ice, -24 °C). The yield of the peptide was significantly improved by the use of the carbamoylmethyl (Cam) ester as the acyl donor instead of the conventional ethyl ester. The peptide yield increased up to ca. 90% when N-benzyloxycarbonyl (CBZ)-Phe-OCam and H-Phe-NH2 were used as the acyl donor and nucleophile, respectively. Such an improvement of the peptide yield in ice was also observed in the coupling of other CBZ-amino acid Cam esters as acyl donors. Furthermore, this approach was applied to the synthesis of peptides containing d-amino acids. The peptides such as CBZ-d-Phe-Phe-NH2, CBZ-Phe-d-Phe-NH2 and CBZ-d-Phe-d-Phe-NH2 were also obtained in excellent to moderate yields in ice. A high diastereoselectivity towards the l-l peptide was observed when the racemic amino acid Cam ester was used as the acyl donor in ice.