83522-39-8

Basic information

• Product Name: N^α-(tert-butoxycarbonyl)-L-phenylalanyl-L-tryptophan methyl ester
• Synonyms: N^α-(tert-butoxycarbonyl)-L-phenylalanyl-L-tryptophan methyl ester
• CAS NO: 83522-39-8
• Molecular Weight: 465.549
• Mol File: 83522-39-8.mol

Chemical Properties

• CAS DataBase Reference: N^α-(tert-butoxycarbonyl)-L-phenylalanyl-L-tryptophan methyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: N^α-(tert-butoxycarbonyl)-L-phenylalanyl-L-tryptophan methyl ester(83522-39-8)
• EPA Substance Registry System: N^α-(tert-butoxycarbonyl)-L-phenylalanyl-L-tryptophan methyl ester(83522-39-8)

Safety Data

• Hazardous Substances Data: 83522-39-8(Hazardous Substances Data)

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 7524-52-9 (S)-tryptophan methyl ester hydrochloride 
• 67729-36-6 Boc-Phe-O-COO-isoBu 
• 4299-70-1 L-tryptophan methyl ester 
• 81000-39-7 (S)-2-((tert-butoxycarbonyl)amino)-3-phenylpropanethioic S-acid 
• 73-22-3 L-Tryptophan 

Downstream Products

• 77935-22-9 Z-Asn-Phe-Phe-Trp-OH 
• 24587-41-5 phenylalanyltryptophane 
• 77935-23-0 H-Asn-Phe-Phe-Trp-OH 
• 83522-41-2 Boc-Phe-Trp-Lys-Thr-Phe-OMe 
• 83536-02-1 Boc-Phe-Trp-Lys-Thr-Phe-OH 
• 218785-68-3 (S)-2-{(S)-2-[(2-Bromo-ethyl)-(2-nitro-benzenesulfonyl)-amino]-3-phenyl-propionylamino}-3-(1H-indol-3-yl)-propionic acid methyl ester 
• 218785-74-1 (S)-2-[(S)-3-Benzyl-4-(2-nitro-benzenesulfonyl)-2-oxo-piperazin-1-yl]-3-(1H-indol-3-yl)-propionic acid methyl ester 
• 218785-62-7 (S)-3-(1H-Indol-3-yl)-2-[(S)-2-(2-nitro-benzenesulfonylamino)-3-phenyl-propionylamino]-propionic acid methyl ester 
• 255378-73-5 Boc-Arg(NO₂)-Pro-Pro-Val-Pro-Phe-Trp-OMe 
• 211426-92-5 Boc-Pro-Pro-Val-Pro-Phe-Trp-OMe 
• 211426-90-3 Boc-Val-Pro-Phe-Trp-OMe 

Relevant articles and documents

Design and synthesis of short amphiphilic cationic peptidomimetics based on biphenyl backbone as antibacterial agents

Antimicrobial peptides (AMPs) and their synthetic mimics have received recent interest as new alternatives to traditional antibiotics in attempts to overcome the rise of antibiotic resistance in many microbes. AMPs are part of the natural defenses of most living organisms and they also have a unique mechanism of action against bacteria. Herein, a new series of short amphiphilic cationic peptidomimetics were synthesized by incorporating the 3′-amino-[1,1′-biphenyl]-3-carboxylic acid backbone to mimic the essential properties of natural AMPs. By altering hydrophobicity and charge, we identified the most potent analogue 25g that was active against both Gram-positive Staphylococcus aureus (MIC = 15.6 μM) and Gram-negative Escherichia coli (MIC = 7.8 μM) bacteria. Cytoplasmic permeability assay results revealed that 25g acts primarily by depolarization of lipids in cytoplasmic membranes. The active compounds were also investigated for their cytotoxicity to human cells, lysis of lipid bilayers using tethered bilayer lipid membranes (tBLMs) and their activity against established biofilms of S. aureus and E. coli.

Copper-Promoted N-Arylation of the Indole Side Chain of Tryptophan Using Triarylbismuthines

A simple protocol for the regioselective N-arylation of the indole side chain of tryptophan using triarylbismuth reagents as the arylating agent is reported. The reaction is catalyzed by copper(II) acetate, and operates in the presence of triethylamine or

Catalytic dehydrative peptide synthesis with gem-diboronic acids

Alkane-gem-diboronic acids have emerged as versatile organoboron catalysts for dehydrative amidation of α-Amino acids. A phenol-substituted multiboron catalyst with a B-C-B structure outperformed simple arylboronic acids in the condensation of α-Amino acids with suppressed epimerization of electrophiles. gem-diboronic acid catalysis were compatible with various O, N, and S-functionalized α-Amino acids bearing N-protecting groups including common carbamates used in peptide synthesis (Boc, Cbz, Fmoc). N-Trifluoroacetyl protection enabled an unprecedented catalytic dehydrative peptide synthesis at room temperature. Preliminary mechanistic studies revealed carboxylate-binding nature of gem-diboronic acids, orthogonal to the activation of carboxylic acids by arylboronic acids. The distinctive reactivity of the gem-diboronic acids would open prospects for mild catalytic peptide condensation.

MITHRAMYCIN DERIVATIVES HAVING INCREASED SELECTIVITY AND ANTI-CANCER ACTIVITY

Mithramycin side chain carboxylic acid (MTM-SA) derivative are provided, which include a substituted amino acid derivative, a substituted amino acid dipeptide derivative, or an unsubstituted dipeptide derivative. The MTM-SA derivatives are useful for treatment of cancer or neuro-diseases associated with an aberrant erythroblast transformation-specific transcription factor. Unique MTM-SA derivatives have increased selectively toward ETS transcription factor.

Development of Mithramycin Analogues with Increased Selectivity toward ETS Transcription Factor Expressing Cancers

Mithramycin A (1) was identified as the top potential inhibitor of the aberrant ETS transcription factor EWS-FLI1, which causes Ewing sarcoma. Unfortunately, 1 has a narrow therapeutic window, compelling us to seek less toxic and more selective analogues. Here, we used MTMSA (2) to generate analogues via peptide coupling and fragment-based drug development strategies. Cytotoxicity assays in ETS and non-ETS dependent cell lines identified two dipeptide analogues, 60 and 61, with 19.1- and 15.6-fold selectivity, respectively, compared to 1.5-fold for 1. Importantly, the cytotoxicity of 60 and 61 is 100 nM in ETS cells. Molecular assays demonstrated the inhibitory capacity of these analogues against EWS-FLI1 mediated transcription in Ewing sarcoma. Structural analysis shows that positioning the tryptophan residue in a distal position improves selectivity, presumably via interaction with the ETS transcription factor. Thus, these analogues may present new ways to target transcription factors for clinical use.

Facile Cu(ii)-mediated conjugation of thioesters and thioacids to peptides and proteins under mild conditions

The bioconjugation of peptide derivatives such as polypeptides, peptide-based probes and proteins is a vibrant area in many scientific fields. However, reports on metal-mediated chemical methods towards native peptides especially non-engineering protein modification under mild conditions are still limited. Herein, we describe a novel Cu(ii)-mediated strategy for the conjugation of thioesters/thioacids to peptides under mild conditions with high functional group tolerance. Based on this strategy, polypeptides, even peptide-based fluorescent probes, can be efficiently constructed. Finally, the selective modification of lysine residues of native Ub with thioesters could be realized and complete conjugation of Ub could be achieved even under equivalent Cu(ii). These promising results could greatly expand Cu(ii)-mediated reaction strategies on chemical biology and molecular imaging.

Synthesis and Biological Evaluations of a Series of Thaxtomin Analogues

Thaxtomins are a unique family of phytotoxins with unique 4-nitroindole and diketopiperazine fragments possessing potential herbicidal activities. This work presents the total synthesis of natural product thaxtomin C and its analogues. The extensive struc

Ultrasound-assisted synthesis and biological evaluation of 1,4-benzodioxane-2-carboxyl-amino acids and Peptides

A series of peptides containing 1,4-benzodioxane nucleus were attempted to synthesize by conventional as well as green techniques like microwave-assisted and sonication, using dicyclohexylcarbodiimide (DCC) as a coupling reagent and triethylamine as a bas

A traceless approach to amide and peptide construction from thioacids and dithiocarbamate-terminal amines

A novel and traceless strategy has been devised that allows a coupling of thioacids and dithiocarbamate-terminal amines. This strategy had been assumed to be dependent on the attachment of a functional equivalent of a cysteine side chain in earlier native chemical ligation approaches. This approach enables the traceless removal of CS2 to directly generate the desired amide bond and is compatible with a range of unprotected side chains of amino acid. The ability to produce amide or peptides by a traceless removal of the auxiliary is a significant virtue of the method. Meanwhile, the application of this new peptide-bond-forming reaction to the synthesis of novel endomorphin (EM) derivatives with various binding potencies was realized.

Novel β-carboline-tripeptide conjugates attenuate mesenteric ischemia/reperfusion injury in the rat

We have synthesized a series of new β-carboline-tripeptide conjugates, and examined their anti-inflammatory properties in a mouse model of xylene-induced ear edema. The analgesic capacity of these compounds was further evaluated in a rodent tail flick ass