78816-88-3

Usage

InChI:InChI=1/C23H28N2O5S/c1-29-22(27)19(13-14-31-2)24-21(26)20(15-17-9-5-3-6-10-17)25-23(28)30-16-18-11-7-4-8-12-18/h3-12,19-20H,13-16H2,1-2H3,(H,24,26)(H,25,28)

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 2491-18-1 (S)-methyl 2-amino-4-(methylthio)butanoate hydrochloride 
• 63-68-3 L-methionine 
• 63-91-2 L-phenylalanine 
• 93605-54-0 (S)-methyl 2-(1H-imidazole-1-carboxamido)-4-(methylthio)butanoate 
• 87072-42-2 Z-L-phenylalanine DCHA salt 
• 10332-17-9 Met-OMe 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 94775-95-8 Z-Phe-Met-NH_.i-C₃H₇ 
• 13126-07-3 Cbz-L-Phe-L-Met-OH 

Relevant academic research and scientific papers

C(sp3)?H Cyanation Promoted by Visible-Light Photoredox/Phosphate Hybrid Catalysis

Inspired by the reaction mechanism of photo-induced DNA cleavage in nature, a C(sp3)?H cyanation reaction promoted by visible-light photoredox/phosphate hybrid catalysis was developed. Phosphate radicals, generated by one-electron photooxidation of phosphate salt, functioned as a hydrogen-atom-transfer catalyst to produce nucleophilic carbon radicals from C(sp3)?H bonds with a high bond-dissociation energy. The resulting carbon radicals were trapped by a cyano radical source (TsCN) to produce the C?H cyanation products. Due to the high functional-group tolerance and versatility of the cyano group, the reaction will be useful for realizing streamlined building block syntheses and late-stage functionalization of drug-like molecules.

Sequential One-Pot Synthesis of Dipeptides through the Transient Formation of CDI-N-Protected α-Aminoesters

The synthesis of dipeptides through a sequential one-pot procedure from commercially available protected amino acids is described. The transformation relies on the use of in situ generated transiently CDI-protected α-amino esters (CDI, e.g. N,N′-carbonyldiimidazole). In addition of being a highly atom-economical process, the couplings take place under very mild and neutral conditions without adding a base to the reaction medium. This protocol provides a concise and less costly route to dipeptide derivatives (12 examples, up to 87% yield) and is compatible with commonly used N-urethane protecting groups. Moreover, no epimerization was detected even when sensitive Boc-Cys(Bn)?OH was used. (Figure presented.).

Inverse peptide synthesis via activated α-aminoesters

A mild, practical, and simple procedure for peptide-bond formation is reported. Instead of activation of the carboxylic acid functionality, the reaction involves an unprecedented use of activated α-aminoesters. The method provides a straightforward entry to dipeptides and was effective when a sensitive cysteine residue was used, as no epimerization was detected in this case. The applicability of this method to iterative peptide synthesis was illustrated by the synthesis of a model tetrapeptide in the challenging reverse N→C direction. How to advance by going into reverse: In a mild and practical procedure for peptide-bond formation, free α-aminoesters were activated by treatment with N,N′-carbonyldiimidazole, instead of activating the carboxylic acid functionality (see scheme). The method provided a straightforward route to dipeptides, and its applicability to iterative peptide synthesis was illustrated by the synthesis of a tetrapeptide in the challenging reverse N→C direction.

Fluorous Coupling Reagents: Application of 2-Chloro-4,6- bis[(heptadecafluorononyl)oxy]-1,3,5-triazine in Peptide Synthesis

Benzyloxycarbonyl N-protected and C-terminus methyl ester protected amino acids react in THF in the presence of 4-methylmorpholine and fluorous condensation reagent, 2-chloro-4,6-bis[(heptadecafluorononyl)oxy[-1,3,5- triazine, to form di- and tripeptides

KINETICS OF THE ALKALINE HYDROLYSIS OF SEVERAL N-BENZYLOXYCARBONYLDIPEPTIDE METHYL AND ETHYL ESTERS

The reaction rates of the alkaline hydrolysis of synthesized N-protected dipeptide methyl and ethyl esters were studied systematically.From the kinetic data the energies of activation, the pre-exponential factors and the reference values at 40 deg C were calculated.The rate of hydrolysis shows to be strongly dependent on the C-terminal amino acid in the sequence Gly >> Ala/Met/Phe > Leu >> Val/Pro.Surprisingly the N-terminal amino acid also exerts an effect, but in a different sequence.N-Terminal Phe in particular shows a relative accelerating effect.Remarkable is the significantly faster ester hydrolysis of glycine containing dipeptide ethyl esters in ethanol/water compared to the corresponding methyl esters in methanol/water.

ETUDE DE LA RACEMISATION INDUITE PAR LA DMAP DANS LES REACTIONS DE COUPLAGE PEPTIDIQUE

The scope and limitation for the use of 4-dimethyalmino pyridine (DMAP) as additive to carbodiimides in peptide synthesis are studied and compared with the results obtained with N-hydroxybenzotriazole (HOBt).The activation of N-acylated aminoacids by the

Design and Synthesis of Enkephalin Analogues: Part I - Synthesis of Met-Enkephalin Alkylamides with Enhanced Analgesic Potency

Synthesis of a series of alkylamides of Met-enkephalin has been achieved employing the key intermediate Boc-Tyr-Gly-Gly-Phe-Met-ONBzl (IV), obtained from Met-ONBzl by treatment with appropiate Nα-Boc-amino acid-2,4,5-trichlorophenyl esters in a