13122-87-7

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 21685-51-8 D-phenylalanine methyl ester 
• 13033-84-6 D-phenylalanine methyl ester hydrochloride 
• 15028-44-1 DL-phenylalanine methyl ester 
• 96452-48-1 benzyl pyridin-2-yl carbonate 
• 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 
• 501-53-1 benzyl chloroformate 

Downstream Products

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

Relevant academic research and scientific papers

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

Catalytic role of PPh3 and its polymer bound analog in the amidation of carboxylic acids mediated by 2,4,6-trichloro-1,3,5-triazine

Abstract The catalytic role of PPh3 and its polymer bound analog was investigated in the 2,4,6-trichloro-1,3,5-triazine (TCT) mediated amidation of carboxylic acids. In the presence of inorganic bases which were inert toward TCT, carboxylic acids rapidly reacted with amines to afford amides in good to excellent yields. The described method also enabled the synthesis of optically active protected dipeptides without racemization. Formation of triazinylphosphonium chloride during the PPh3 catalyzed acid activation was confirmed based on 31P NMR studies.

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.

Stereoselective self-sorting in the self-assembly of a Phe-Phe extended guanidiniocarbonyl pyrrole carboxylate zwitterion: Formation of two diastereomeric dimers with significantly different stabilities

The 'dipeptide extended' guanidiniocarbonyl pyrrole carboxylate zwitterion GCP-Phe-Phe 1 forms stable dimers in DMSO. However, dimerization is highly stereoselective. Only homochiral dimers are formed and the (L,L)·(L,L) dimer (Kdim > 105 M-1) is significantly more stable by a factor of 103 than the diastereomeric (D,L)·(D,L) dimer (Kdim = 120 M-1).

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.

Enantioselection in peptide bond formation

Selectivity in abiotic condensations of amino acids remains controversial and stereochemically little explored. We find that competitive activated couplings of N-acyl derivatives of glycine, alanine, valine, proline and phenylalanine with binary, ternary and quaternary mixtures of amides and esters of the same group of amino acids show little selectivity among the reactants, except with respect to configuration, where a consistent and significant preference for heterochiral outcomes, mostly >80%, is observed. One possible explanation of this selectivity predicts a predisposition to homochiral coupling under conditions that would require the two carboxyl functions to be co-facial in the activated complex.

Efficient 1,4-Asymetric Induction Utilizing Electrostatic Interaction between Ligand and Substrate in the Asymmetric Hydrogenation of Didehydrodipeptides

Electrostatic interaction between the amino group of the achiral 3-dimethylaminopropylidenebismethylenebis(diphenylphosphine) (1) and the carboxy group of the substrate enable an effective 1,4-asymmetric induction in the RhI-catalysed hydrogenation of didehydrodipeptides, to give (S,S)-or (R,R)-products selectively.The selectivity reached up to 94percent diastereoisomeric excess with acetyl didehydrodipeptides and 92percent with benzyloxycarbonyl substrates.

2(1H)-Pyridone as Leaving Group in Acylation Reactions - Applications in Peptide Synthesis

Alkyl 2-pyridyl carbonates 3 or mixtures of 3 and the isomeric N-(alkoxycarbonyl)-2-pyridones 3' are useful for the introduction of urethane protective groups into amino acids.The N-protected amino acids 7 - 10 react with 2(1H)-pyridone (1a) using the carbodiimide method to yield 2-pyridyl active esters 11, which easily undergo coupling reactions with amino acid esters 12 with elimination of 1a to give peptides 13 in good yields as well as high optical purities.