74193-68-3

Usage

Uses

Used in Pharmaceutical Industry:
L-Leucine, N-[N-[(1,1-dimethylethoxy)carbonyl]-L-phenylalanyl]-, phenylmethyl ester is used as a building block for the synthesis of various drugs and peptides. Its unique structure allows for the creation of new compounds with potential therapeutic applications.
Used in Sports Supplements:
L-Leucine, N-[N-[(1,1-dimethylethoxy)carbonyl]-L-phenylalanyl]-, phenylmethyl ester is used as an ingredient in sports supplements for its ability to enhance protein synthesis and muscle growth. This makes it a popular choice for athletes and individuals looking to improve their physical performance.
Used in Metabolic Disorders Management:
L-Leucine, N-[N-[(1,1-dimethylethoxy)carbonyl]-L-phenylalanyl]-, phenylmethyl ester is being studied for its potential role in improving insulin sensitivity and managing metabolic disorders. Its effects on these conditions are still under investigation, but early research suggests it may offer benefits for individuals with certain health issues.

Upstream product

• 1738-69-8 L-Leucine benzyl ester 
• 112695-92-8 Boc-Phe-OH 2,6-dibromo-4-sulfenyl ester sodium salt 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 1738-77-8 L-leucine benzyl ester p-toluenesulfonate 
• 7535-56-0 N-t-butoxycarbonyl-L-phenylalanine 4-nitrophenyl ester 
• 7517-19-3 methyl (L)-leucinate hydrochloride 
• 64152-76-7 methyl (S)-2-((S)-2-(tert-butoxycarbonylamino)-3-phenylpropanamido)-4-methylpentanoate 
• 100-51-6 benzyl alcohol 
• 5557-81-3 L-alanine benzyl ester hydrochloride 
• 1738-77-8 tosylate of leucine benzyl ester 
• 4530-18-1 N-(tert-butoxycarbonyl)-L-phenylalanine 
• 87746-56-3 2-tert-butoxycarbonylamino-4-methyl-penatnoic acid benzyl ester 
• 24424-99-5 di-tert-butyl dicarbonate 
• 63-91-2 L-phenylalanine 

Downstream Products

• 73994-88-4 Boc-Gly-Phe-Leu-OBzl 
• 63649-15-0 L-phenylalanyl-L-leucine benzyl ester 
• 73994-87-3 (S)-benzyl 2-((S)-2-amino-3-phenylpropanamido)-4-methylpentanoate hydrochloride 
• 74193-69-4 N-tert-butyloxycarbonyl-L-phenylalanyl-L-leucine hydrazide 
• 88621-25-4 Boc-Phet-Leu-OBzl 
• 69729-14-2 benzyl ester of N-tert-butoxycarbonylglycylglycylphenylalanylleucine 
• 73994-90-8 glycyl-L-phenylalanyl-L-leucine benzyl ester p-toluenesulfonate 
• 77066-56-9 benzyl-L-penylalanyl-L-leucinate trifluoroacetic acid 
• 1365292-48-3 L-isoseryl-L-phenylalanyl-L-leucine benzyl ester hydrochloride 
• 1365292-56-3 C₁₈H₂₇N₃O₅*ClH 
• 77511-32-1 5>-enkephalin 
• 64963-27-5 N-tert-butyloxycarbonyl-L-tyrosyl-glycyl-glycyl-L-phenylalanyl-L-leucine 
• 63986-20-9 HCl·H-Tyr(OH)-Gly-Gly-Phe-Leu-OH 
• 1250884-46-8 methyl N-(tert-butyloxycarbonyl)-(S)-phenylalanyl-(RS)-leucinate 

Relevant academic research and scientific papers

NDTP Mediated Direct Rapid Amide and Peptide Synthesis without Epimerization

Herein, we explored an unprecedented mild, nonirritating, conveniently available, and recyclable coupling reagent NDTP, which could activate the carboxylic acids via acyl thiocyanide and enable the rapid amide and peptide synthesis at very mild conditions

The photoredox-catalyzed hydrosulfamoylation of styrenes and its application in the novel synthesis of naratriptan

The hydrosulfamoylation of diverse aryl olefins provides facile access to alkylsulfonamides. Here we report a novel protocol utilizing radical-mediated addition and a thiol-assisted strategy to achieve the hydrosulfamoylation of diverse styrenes in modest to excellent yields under mild and economic reaction conditions. The methodology was found to provide an efficient and convenient approach for the synthesis of the anti-migraine drug naratriptan and it also can be used for the late-stage functionalization of natural products or medicines.

METHOD FOR PRODUCING CARBOXYLIC ACID AMIDE COMPOUND, AND CATALYST AND FLOW PRODUCTION SYSTEM

PROBLEM TO BE SOLVED: To provide a new production method that allows a dehydration condensation reaction between carboxylic acid and amine, and a catalyst. SOLUTION: A method for producing a carboxylic acid amide compound includes the step for causing a r

New cysteine protease inhibitors: Electrophilic (Het)arenes and unexpected prodrug identification for the trypanosoma protease rhodesain

Electrophilic (het)arenes can undergo reactions with nucleophiles yielding π- or Meisenheimer (σ-) complexes or the products of the SNAr addition/elimination reactions. Such building blocks have only rarely been employed for the design of enzyme inhibitors. Herein, we demonstrate the combination of a peptidic recognition sequence with such electrophilic (het)arenes to generate highly active inhibitors of disease-relevant proteases. We further elucidate an unexpected mode of action for the trypanosomal protease rhodesain using NMR spectroscopy and mass spectrometry, enzyme kinetics and various types of simulations. After hydrolysis of an ester function in the recognition sequence of a weakly active prodrug inhibitor, the liberated carboxylic acid represents a highly potent inhibitor of rhodesain (Ki = 4.0 nM). The simulations indicate that, after the cleavage of the ester, the carboxylic acid leaves the active site and re-binds to the enzyme in an orientation that allows the formation of a very stable π-complex between the catalytic dyad (Cys-25/His-162) of rhodesain and the electrophilic aromatic moiety. The reversible inhibition mode results because the SNAr reaction, which is found in an alkaline solvent containing a low molecular weight thiol, is hindered within the enzyme due to the presence of the positively charged imidazolium ring of His-162. Comparisons between measured and calculated NMR shifts support this interpretation.

Naphthoquinones as covalent reversible inhibitors of cysteine proteases—studies on inhibition mechanism and kinetics

The facile synthesis and detailed investigation of a class of highly potent protease inhibitors based on 1,4‐naphthoquinones with a dipeptidic recognition motif (HN‐L‐Phe‐L‐Leu‐OR) in the 2‐position and an electron‐withdrawing group (EWG) in the 3‐positio

Method of producing peptide

The present invention is related to a method of producing a peptide, characterized in contacting a reaction mixture with a base after a condensation reaction to hydrolyze while a basic condition is maintained until a ratio of a remaining unreacted active

Synthesis of a novel series of L-isoserine derivatives as aminopeptidase N inhibitors

A series of novel L-isoserine derivatives were synthesised and evaluated for their ability to inhibit aminopeptidase N (APN)/CD13. In our preliminary biological results, some of these compounds possessed a potent inhibitory activity against the APN. Within this series, compound 14b not only showed similar enzyme inhibition (IC50 of 12.2μM) compared with the positive control bestatin (half maximal inhibitory concentration (IC 50) of 7.3μM), but also had a potent antiproliferative activity against human cancer cell lines cells.

Preparation and conformational study of CF3-containing enkephalin-derived oligopeptide

Incorporation of (2S,3S)-4,4,4-trifluorothreonine (F3-Thr) instead of Thr in the enkephalin-derived hexapeptide led to the apparent conformational alteration due to the strong electron-withdrawing effect of the trifluoromethyl group by comparison with the original compound on the basis of their various NMR measurements.

Introduction of F3-Threonine to the Hexapeptide, DSLET: Investigation of the Effect of Fluorine Atoms toward Peptidic Conformations

Introduction of trifluoromethyl-containing threonine to the target hexapeptide, Tyr-D-Ser-Gly-Phe-Leu-Thr (DSLET), led to the apparent conformational alteration due to the electron-withdrawing effect of the CF 3 group when compared with the ori

MW-enhanced high-speed deprotection of Boc group using p-TsOH and concommitant formation of N-Me-amino acid benzyl ester p-TsOH salts

A high-speed, complete deprotection of Boc group from Boc amino acids and protected peptide esters employing p-TsOH in toluene under microwave irradiation is found to be complete in 30s. The deprotection can be carried out in methanol and acetonitrile also. Under the present conditions, C-peptide benzyl esters and O-benzyl ethers have been found to be stable. This has permitted us to carry out the synthesis of [Leu]enkephalin employing the Boc/Bzl-group strategy. Further more, it has been found that both Nα-Fmoc and N α-Z groups are completely stable. The present conditions can be extended for the concomitant removal of the Boc group and the formation of C-benzyl amino acid esters as well. This has been utilized for the synthesis of N-Me amino acid benzyl esters starting from Boc-N-Me amino acids in a single step. Copyright Taylor & Francis, Inc.