7432-21-5

Basic information

• Product Name: N-Cbz-L-Tryptophan
• Synonyms: BENZYLOXYCARBONYL-L-TRYPTOPHAN;CBZ-TRP-OH;CBZ-L-TRYPTOPHAN;Z-L-TRP-OH;Z-L-TRYPTOPHAN;Z-TRYPTOPHAN;Z-TRP-OH;N-CARBOBENZOXY-L-TRYPTOPHAN
• CAS NO: 7432-21-5
• Molecular Formula: C₁₉H₁₈N₂O₄
• Molecular Weight: 338.36
• EINECS: 231-074-4
• Product Categories: AMINOACIDS DERIVATIVES;Tryptophan [Trp, W];Z-Amino Acids and Derivatives;Amino Acids;Amino Acids (N-Protected);Biochemistry;Cbz-Amino Acids;Indoles;Tryptophans;Cbz-Amino acid series
• Mol File: 7432-21-5.mol

Chemical Properties

• Melting Point: 124-127 °C(lit.)
• Boiling Point: 474.51°C (rough estimate)
• Flash Point: 328.2 °C
• Appearance: white to light yellow crystal powder powder
• Density: 1.2855 (rough estimate)
• Vapor Pressure: 3.46E-16mmHg at 25°C
• Refractive Index: 1.6140 (estimate)
• Storage Temp.: 2-8°C
• Solubility: methanol: 0.1 g/mL, clear
• PKA: 3.98±0.10(Predicted)
• BRN: 96743
• CAS DataBase Reference: N-Cbz-L-Tryptophan(CAS DataBase Reference)
• NIST Chemistry Reference: N-Cbz-L-Tryptophan(7432-21-5)
• EPA Substance Registry System: N-Cbz-L-Tryptophan(7432-21-5)

Safety Data

• Hazard Codes: Xn
• Statements: 20/21/22-36/37/38
• Safety Statements: 22-24/25-36-26
• WGK Germany: 3
• Hazardous Substances Data: 7432-21-5(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
N-Cbz-L-Tryptophan is used as an intermediate in the synthesis of various pharmaceutical compounds due to its role as a protected form of L-Tryptophan. It aids in the development of drugs targeting cell proliferation and protein biosynthesis.
Used in Research and Development:
N-Cbz-L-Tryptophan is utilized as a research compound for studying the role of L-Tryptophan in cell proliferation, protein biosynthesis, and its involvement in the production of Serotonin. It is also used to investigate the potential link between L-Tryptophan and eosinophilia-myalgia syndrome.
Used in Chemical Synthesis:
N-Cbz-L-Tryptophan is employed as a building block in the chemical synthesis of various organic compounds, taking advantage of its protected structure to facilitate specific reactions and improve the overall yield of the desired products.
Used in Nutritional Supplements:
Although not explicitly mentioned in the provided materials, N-Cbz-L-Tryptophan could potentially be used in the development of nutritional supplements, given its connection to L-Tryptophan, which is known for its importance in protein synthesis and its role in the production of Serotonin.

InChI:InChI=1/C19H18N2O4/c22-18(23)17(10-14-11-20-16-9-5-4-8-15(14)16)21-19(24)25-12-13-6-2-1-3-7-13/h1-9,11,17,20H,10,12H2,(H,21,24)(H,22,23)/p-1/t17-/m0/s1

Upstream product

• 501-53-1 benzyl chloroformate 
• 73-22-3 L-Tryptophan 
• 31139-36-3 dibenzyl dicarbonate 
• 91285-94-8 O-benzyl S-(pyridin-2-yl)carbonothioate 
• 107292-10-4 2-Benzyloxycarbonyloxy-3,6-diisopropylpyrazine 
• 107292-14-8 Benzyl S-3,6-diisopropylpyrazin-2-ylthiolcarbonate 
• 96452-48-1 benzyl pyridin-2-yl carbonate 
• 73-22-3 L-tryptophan 
• 75819-24-8 3-benzyloxycarbonyl-2-oxazolone 
• 2717-76-2 (S)-N-benzyloxycarbonyl-L-tryptophan methyl ester 
• 7524-52-9 (S)-tryptophan methyl ester hydrochloride 
• 61668-49-3 sodium benzylcarbonate 
• 16624-64-9 N-α-carbobenzoxy-L-tyrosine p-nitrophenyl ester 
• 69876-37-5 (S)-benzyl 2-(((benzyloxy)carbonyl)amino)-3-(1H-indol-3-yl)propanoate 

Downstream Products

• 17689-58-6 N-(benzyloxycarbonyl)-L-tryptophanyl-L-tryptophan methyl ester 
• 81444-75-9 N-(benzyloxycarbonyl)-L-tryptophanyl-D-tryptophan methyl ester 
• 127130-93-2 N-(benzyloxycarbonyl)-L-tryptophane (3-methyl-3-oxetanyl)methyl ester 
• 76413-59-7 [(S)-1-(1H-Indol-3-ylmethyl)-2-oxo-2-(2-thioxo-thiazolidin-3-yl)-ethyl]-carbamic acid benzyl ester 
• 50305-28-7 Cbz-L-Tryptophan-OSu 
• 13673-49-9 Z-Trp-OPcp 
• 16874-03-6 N-[(phenylmethoxy)carbonyl]-L-tryptophan 1,1-dimethylethyl ester 
• 133808-25-0 [(S)-2-[(4-Chloro-benzoyl)-methyl-aminooxy]-1-(1H-indol-3-ylmethyl)-2-oxo-ethyl]-carbamic acid benzyl ester 
• 65864-26-8 Z-Trp-Nle-Asp(OBzl)-Phe-NH₂ 
• 52574-27-3 Nα-Benzyloxycarbonyl-L-tryptophyl-L-serine methyl ester 
• 111237-83-3 N^α-(benzyloxycarbonyl)tryptophanyl-N^ε-(benzyloxycarbonyl)lysine methyl ester 
• 2279-10-9 Z-Trp-Gly-OMe 
• 55782-87-1 N-carbobenzyloxy-L-tryptophanyl-L-proline methyl ester 
• 74992-61-3 N-carbobenzyloxy-L-tryptophanyl-L-proline p-nitrophenyl ester 

Relevant articles and documents

Synthesis and evaluation of oxindoles as promising inhibitors of the immunosuppressive enzyme indoleamine 2,3-dioxygenase 1

Indoleamine 2,3-dioxygenase 1 (IDO1) is considered as an important therapeutic target for the treatment of cancer, chronic infections and other diseases that are associated with immune suppression. Recent developments in understanding the catalytic mechanism of the IDO1 enzyme revealed that conversion of l-tryptophan (l-Trp) to N-formylkynurenine proceeded through an epoxide intermediate state. Accordingly, we synthesized a series of 3-substituted oxindoles from l-Trp, tryptamine and isatin. Compounds with C3-substituted oxindole moieties showed moderate inhibitory activity against the purified human IDO1 enzyme. Their optimization led to the identification of potent compounds, 6, 22, 23 and 25 (IC50 = 0.19 to 0.62 μM), which are competitive inhibitors of IDO1 with respect to l-Trp. These potent compounds also showed IDO1 inhibition potencies in the low-micromolar range (IC50 = 0.33-0.49 μM) in MDA-MB-231 cells. The cytotoxicity of these potent compounds was trivial in different model cancer (MDA-MB-231, A549 and HeLa) cells and macrophage (J774A.1) cells. Stronger selectivity for the IDO1 enzyme (124 to 210-fold) over the tryptophan 2,3-dioxygenase (TDO) enzyme was also observed for these compounds. These results suggest that the oxindole moiety of the compounds could mimic the epoxide intermediate state of l-Trp. Therefore, the structural simplicity and low-micromolar inhibition potencies of these 3-substituted oxindoles make them quite attractive for further investigation of IDO1 function and immunotherapeutic applications.

C ring may be dispensable for β-carboline: Design, synthesis, and bioactivities evaluation of tryptophan analog derivatives based on the biosynthesis of β-carboline alkaloids

According to our previous work and the latest research on the biosynthesis of β-carboline, and using the reverse thinking strategy, tryptophan, the biosynthesis precursor of β-carboline alkaloids, and their derivatives were synthesized, and their biological activities and structure-activity relationships were studied. This bioassay showed that these compounds exhibited good inhibitory activities against tobacco mosaic virus (TMV); especially (S)-2-amino-3-(1H-indol-3-yl)-N-octylpropanamide (4) (63.3 ± 2.1%, 67.1 ± 1.9%, 68.7 ± 1.3%, and 64.5 ± 3.1%, 500 μg/mL) exhibited the best antiviral activity both in vitro and in vivo. Compound 4 was chosen for the field trials and the acute oral toxicity test, the results showed that the compound exhibited good anti-TMV activity in the field and low acute oral toxicity. We also found that these compounds showed antifungal activities and insecticidal activities.

Tryptophan derivative, preparing method and application in preventing and treating plant viruses, killing bacteria and killing insects

The invention relates to a tryptophan derivative (I), a preparing method of the tryptophan derivative (I), and application of the tryptophan derivative (I) in preventing and treating plant viruses, killing bacteria and killing insects. The formula of the tryptophan derivative (I) is shown in the description, and the meanings of all groups in the formula are shown in the description. The tryptophan derivative expresses especially excellent plant virus resisting activity, and also has broad-spectrum bactericidal activity and insecticidal activity.

LAT1 activity of carboxylic acid bioisosteres: Evaluation of hydroxamic acids as substrates

Large neutral amino acid transporter 1 (LAT1) is a solute carrier protein located primarily in the blood–brain barrier (BBB) that offers the potential to deliver drugs to the brain. It is also up-regulated in cancer cells, as part of a tumor's increased metabolic demands. Previously, amino acid prodrugs have been shown to be transported by LAT1. Carboxylic acid bioisosteres may afford prodrugs with an altered physicochemical and pharmacokinetic profile than those derived from natural amino acids, allowing for higher brain or tumor levels of drug and/or lower toxicity. The effect of replacing phenylalanine's carboxylic acid with a tetrazole, acylsulfonamide and hydroxamic acid (HA) bioisostere was examined. Compounds were tested for their ability to be LAT1 substrates using both cis-inhibition and trans-stimulation cell assays. As HA-Phe demonstrated weak substrate activity, its structure–activity relationship (SAR) was further explored by synthesis and testing of HA derivatives of other LAT1 amino acid substrates (i.e., Tyr, Leu, Ile, and Met). The potential for a false positive in the trans-stimulation assay caused by parent amino acid was evaluated by conducting compound stability experiments for both HA-Leu and the corresponding methyl ester derivative. We concluded that HA's are transported by LAT1. In addition, our results lend support to a recent account that amino acid esters are LAT1 substrates, and that hydrogen bonding may be as important as charge for interaction with the transporter binding site.

Synergism between genome sequencing, tandem mass spectrometry and bio-inspired synthesis reveals insights into nocardioazine B biogenesis

Marine actinomycete-derived natural products continue to inspire chemical and biological investigations. Nocardioazines A and B (3 and 4), from Nocardiopsis sp. CMB-M0232, are structurally unique alkaloids featuring a 2,5-diketopiperazine (DKP) core functionalized with indole C3-prenyl as well as indole C3- and N-methyl groups. The logic of their assembly remains cryptic. Bioinformatics analyses of the Nocardiopsis sp. CMB-M0232 draft genome afforded the noz cluster, split across two regions of the genome, and encoding putative open reading frames with roles in nocardioazine biosynthesis, including cyclodipeptide synthase (CDPS), prenyltransferase, methyltransferase, and cytochrome P450 homologs. Heterologous expression of a twelve gene contig from the noz cluster in Streptomyces coelicolor resulted in accumulation of cyclo-l-Trp-l-Trp DKP (5). This experimentally connected the noz cluster to indole alkaloid natural product biosynthesis. Results from bioinformatics analyses of the noz pathway along with challenges in actinomycete genetics prompted us to use asymmetric synthesis and mass spectrometry to determine biosynthetic intermediates in the noz pathway. The structures of hypothesized biosynthetic intermediates 5 and 12-17 were firmly established through chemical synthesis. LC-MS and MS-MS comparison of these synthetic compounds with metabolites present in chemical extracts from Nocardiopsis sp. CMB-M0232 revealed which of these hypothesized intermediates were relevant in the nocardioazine biosynthetic pathway. This established the early and mid-stages of the biosynthetic pathway, demonstrating that Nocardiopsis performs indole C3-methylation prior to indole C3-normal prenylation and indole N1′-methylation in nocardioazine B assembly. These results highlight the utility of merging bioinformatics analyses, asymmetric synthetic approaches, and mass spectrometric metabolite profiling in probing natural product biosynthesis.

Design and synthesis of tryptophan containing dipeptide derivatives as formyl peptide receptor 1 antagonist

Our previous studies identified an Fmoc-(S,R)-tryptophan-containing dipeptide derivative, 1, which selectively inhibited neutrophil elastase release induced by formyl-l-methionyl-l-leucyl-l-phenylalanine (FMLP) in human neutrophils. In an attempt to improve pharmacological activity, a series of tryptophan-containing dipeptides were synthesized and their pharmacological activities were investigated in human neutrophils. Of these, five compounds 3, 6, 19a, 24a, and 24b exhibited potent and dual inhibitory effects on FMLP-induced superoxide anion (O2-) generation and neutrophil elastase release in neutrophils with IC50 values of 0.23/0.60, 1.88/2.47, 1.87/3.60, 0.12/0.37, and 1.32/1.03 μM, respectively. Further studies indicated that inhibition of superoxide production in human neutrophils by these dipeptides was associated with the selective inhibition of formyl peptide receptor 1 (FPR1). Furthermore, the results of structure-activity relationship studies concluded that the fragment N-benzoyl-Trp-Phe-OMe (3) was most suitable as a core structure for interaction with FPR1, and may be approved as a lead for the development of new drugs in the treatment of neutrophilic inflammatory diseases. As some of the synthesized compounds exhibited separable conformational isomers, and showed diverse bioactivities, the conformation analysis of these compounds is also discussed herein. The Royal Society of Chemistry 2013.

A concise preparation of the non-proteinogenic amino acid l-kynurenine

A concise and practical preparation of the non-proteinogenic amino acid l-kynurenine is reported. The synthetic approach is scalable and provides ready access to this valuable amino acid in either l- or d-stereochemistry starting from l- or d-tryptophan, respectively. In the optimized procedure, two discreet oxidation steps are applied sequentially to convert the tryptophan indole ring into the keto-aniline moiety contained within the kynurenine side chain.

Orthogonal protecting groups in the synthesis of tryptophanyl- hexahydropyrroloindoles

The synthesis of various polycyclic systems containing aC 3a-Ni bond between a hexahydropyrrolo[2,3-b]indole and an indole tryptophan is described here. A series of experiments were performed to determine the best combination of five orthogonal protecting groups and the best reaction conditions for formation of said bond, which is a common feature among many recently discovered marine natural products.

PROCESS FOR PREPARING VAPREOTIDE

A solution phase process for preparing vapreotide, having the formula:

Aqueous phase mono-protection of amines and amino acids as N-benzyloxycarbonyl derivatives in the presence of β-cyclodextrin

A simple and selective protection of amines/amino acids with Cbz-Cl has been achieved in aqueous phase with catalytic amounts of β-cyclodextrin in high yields at room temperature. This reaction proceeds without the formation of any by-products and has advantages over existing methods.