13512-31-7

Basic information

• Product Name: Z-TYR-OME
• Synonyms: N-CARBOBENZOXY-L-TYROSINE METHYL ESTER;N-ALPHA-CARBOBENZOXY-L-TYROSINE METHYL ESTER;Z-L-TYROSINE METHYL ESTER;Z-TYR-OME;Z-TYROSINE-OME;CBZ-L-TYROSINE METHYL ESTER;(S)-methyl 2-(benzyloxycarbonylamino)-3-(4-hydroxyphenyl)propanoate;N-Benzyloxycarbonyl-L-tyrosine Methyl ester
• CAS NO: 13512-31-7
• Molecular Formula: C₁₈H₁₉NO₅
• Molecular Weight: 329.35
• EINECS: 1312995-182-4
• Product Categories: AMINOACIDS DERIVATIVES;Z-Amino Acids and Derivatives;Z-Amino acid series;Amino Acid Derivatives;Peptide Synthesis;Tyrosine
• Mol File: 13512-31-7.mol

Chemical Properties

• Melting Point: 93-97 °C(lit.)
• Boiling Point: 528.1 °C at 760 mmHg
• Flash Point: 273.2 °C
• Appearance: /Solid
• Density: 1.249 g/cm³
• Vapor Pressure: 9.06E-12mmHg at 25°C
• Refractive Index: 1.58
• Storage Temp.: -15°C
• PKA: 9.75±0.15(Predicted)
• CAS DataBase Reference: Z-TYR-OME(CAS DataBase Reference)
• NIST Chemistry Reference: Z-TYR-OME(13512-31-7)
• EPA Substance Registry System: Z-TYR-OME(13512-31-7)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 13512-31-7(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Z-TYR-OME is used as an intermediate in the synthesis of optically active imidazolidione derivatives. These derivatives are important in the development of pharmaceuticals with potential applications in various therapeutic areas.
Used in Organic Chemistry:
In the field of organic chemistry, Z-TYR-OME serves as a key building block for the preparation of complex molecules with specific stereochemistry. The compound can be transformed through a series of reactions, including ethylation, reduction, and successive treatment with methanesulfonyl chloride, ethylenediamine, and lithium hydroxide, to obtain the desired imidazolidione derivatives.

InChI:InChI=1/C18H19NO5/c1-23-17(21)16(11-13-7-9-15(20)10-8-13)19-18(22)24-12-14-5-3-2-4-6-14/h2-10,16,20H,11-12H2,1H3,(H,19,22)

Upstream product

• 1080-06-4 L-Tyr-OMe 
• 501-53-1 benzyl chloroformate 
• 67-56-1 methanol 
• 1164-16-5 Z-L-Tyr-OH 
• 186581-53-3 diazomethane 
• 13139-17-8 N-(Benzyloxycarbonyloxy)succinimide 
• 3417-91-2 L-tyrosine methyl ester HCl 
• 5618-98-4 N-α-benzyloxycarbonyl-DL-tyrosine 
• 74-88-4 methyl iodide 
• 19898-39-6 N-Carbobenzyloxy-L-tyrosinamide 
• 86099-14-1 (2S)-3-(4-hydroxyphenyl)-2-(methyl{[(phenylmethyl)oxy]carbonyl}amino)propanoic acid 
• 60-18-4 L-tyrosine 
• 13795-24-9 benzyl 4-nitrophenyl carbonate 
• 4637-24-5 N,N-dimethyl-formamide dimethyl acetal 

Downstream Products

• 51514-13-7 O-acetyl-N-benzyloxycarbonyl L-tyrosine 
• 17331-91-8 N-CBZ-L-Tyr-L-LeuNH₂ 
• 102683-28-3 N-(benzyloxycarbonyl)-L-tyrosyl-D-arginine methyl ester 
• 102683-29-4 N-(benzyloxycarbonyl)-L-tyrosyl-L-arginine methyl ester 
• 102683-26-1 N-(benzyloxycarbonyl)-L-tyrosyl-D-serine methyl ester 
• 38074-71-4 N-Benzyloxycarbonyl-3-methylthiomethyl-tyrosin-methylester 
• 5068-29-1 2-benzyloxycarbonylamino-3-(4-tert-butoxy-phenyl)-propionic acid methyl ester 
• 183021-88-7 methyl 2-{[(benzyloxy)carbonyl]amino}-3-(4-{[(trifluoromethyl)sulfonyl]oxy}phenyl)propanoate 
• 226889-64-1 Pyridine-2,6-dicarboxylic acid bis-[4-((S)-2-benzyloxycarbonylamino-2-methoxycarbonyl-ethyl)-phenyl] ester 
• 226889-65-2 Decanedioic acid bis-[4-((S)-2-benzyloxycarbonylamino-2-methoxycarbonyl-ethyl)-phenyl] ester 
• 226889-63-0 Isophthalic acid bis-[4-((S)-2-benzyloxycarbonylamino-2-methoxycarbonyl-ethyl)-phenyl] ester 
• 132149-66-7 dimethyl 3,3′-(6,6′-dihydroxybiphenyl-3,3′-diyl)bis[2-(benzyloxycarbonylamino)propanoate] 
• 329065-40-9 Z-Isodityr-OMe 
• 374803-71-1 (S)-2-Benzyloxycarbonylamino-3-{4-[2-(5-methyl-2-phenyl-oxazol-4-yl)-ethoxy]-phenyl}-propionic acid methyl ester 

Relevant articles and documents

Synthesis of Carbamates Using Yttria-Zirconia Based Lewis Acid Catalyst

A variety of amines react with chloroformates in the presence of catalytic amount of yttria-zirconia based catalyst to afford the corresponding carbamates in excellent yields.

An efficient, stereocontrolled and versatile synthetic route to bicyclic partially saturated privileged scaffolds

Herein, we describe the development of a simple, high yielding and stereocontrolled strategy for the synthesis of a series of triazolopiperazines and other biologically relevant fused scaffolds from optically active amino acids. This route was applied to the synthesis of 22 scaffolds containing new, previously inaccessible vectors and used to access a novel analogue of ganaplacide.

Tailoring the Substitution Pattern on 1,3,5-Triazine for Targeting Cyclooxygenase-2: Discovery and Structure-Activity Relationship of Triazine-4-Aminophenylmorpholin-3-one Hybrids that Reverse Algesia and Inflammation in Swiss Albino Mice

Here, we report analgesic and anti-inflammatory activity of a series of compounds obtained by appending 4-aminophenylmorpholin-3-one and acyclic, cyclic, or heterocyclic moieties on 1,3,5-triazine. The structures of compounds 4b and 6b are optimized for the best inhibition of COX-2 with IC50 values of 0.06 and 0.08 μM, respectively, and selectivity over COX-1 of 166 and >125, respectively. At the dose of 5 mg kg-1, these compounds significantly reduced acetic acid induced writhings, and their ED50 values were found to be 2.2 and 1.9 mg kg-1, respectively. Besides the cell-based and animal-based experiments showing the modes of action of these compounds targeting COX-2, the interaction behavior of 4b with COX-2 was also characterized, with physicochemical experiments including ITC, NMR, UV-vis, and molecular-modeling studies. Characteristically, these compounds interact with R120, Y355, and W385, the residues responsible for holding the substrate and mediating the process of electron transfer during the metabolic phase of the enzyme.

A N-(9-fluorenylmethyloxycarbonyl)-O-tert-butyl-L-tyrosine method for the preparation of

The invention relates to a method for preparing N-(9-fluorenylmethoxy carbony)-O-tertiary butyl-L-tyrosine. The problem that an enantiomer is easily generated is solved. The method comprises the following synthetic steps: (1) dissolving L-Tyr into a methanol solution, adding SOCl2 and then carrying out reflux reaction, so as to obtain Tyr-OMe.HCl; (2) dissolving the Tyr-OMe.HCl into a water solution, adding AcOEt and Na2CO3 and then reacting with Z-Cl, and controlling the pH of the system at 7-10, so as to obtain Z-L-Tyr-OMe; (3) dissolving the Z-L-Tyr-OMe into a CH2Cl2 solution, adding H2SO4 and isobutene, reacting at normal temperature for 1-10 days, so as to obtain Z-L-Tyr(tBu)-OMe; (4) adding the NaOH solution to the Z-L-Tyr(tBu)-OMe to react, so as to obtain Z-L-Tyr(tBu); (5) dissolving the Z-L-Tyr(tBu) into methanol, adding Pd/C, and leading in hydrogen to react, so as to obtain L-Tyr(tBu); (6) dissolving Z-L-Tyr(tBu) into the water solution, adding the Na2CO3 and THF and then reacting with Fmoc-osu, and controlling the pH of the system at 8-10, so as to obtain Fmoc-Tyr(tBu). By adopting the method, generation of the enantiomer is avoided, and the citric acid is taken as an acidifier, so that the product is more stable, and the reaction processes do not relate to high-temperature and high-pressure reaction, and the method is applicable to large-scale production.

Synthesis, bioactivity, docking and molecular dynamics studies of furan-based peptides as 20s proteasome inhibitors

Proteasome inhibitors are promising compounds for a number of therapies, including cardiovascular and eye diseases, diabetes, and cancers. We previously reported a series of furanbased peptidic inhibitors with moderate potencies against the proteasome b5 subunit, hypothesizing that the C-terminal furyl ketone motif could form a covalent bond with the catalytic residue, threonine 1. In this context, we describe further optimizations of the furan-based peptides, and a series of dipeptidic and tripeptidic inhibitors were designed and synthesized, aiming at improved potency and better solubility. Most of the tripeptidic inhibitors demonstrated improved potency and selectivity as b5 subunit inhibitors in both enzymatic and cellular assays, and good antineoplastic activities in various tumor cell lines were also observed. However, no inhibitory effects were observed for the dipeptidic compounds, which led us to presume that a noncovalent binding mode is adopted. Docking studies and molecular dynamics simulations were carried out to verify this presumption, with results showing that the distance between the furyl ketone motif and Thr1 is slightly too long to form covalent bond.

Highly efficient and selective phosphorylation of amino acid derivatives and polyols catalysed by 2-aryl-4-(dimethylamino)pyridine-N-oxides-towards kinase-like reactivity

The chemoselective phosphorylation of hydroxyl containing amino acid derivatives and polyols by phosphoryl chlorides catalyzed by 2-aryl-4-(dimethylamino)pyridine-N-oxides is described.

One-step C-terminal deprotection and activation of peptides with peptide amidase from stenotrophomonas maltophilia in neat organic solvent

Chemoenzymatic peptide synthesis is a rapidly developing technology for cost effective peptide production on a large scale. As an alternative to the traditional C→N strategy, which employs expensive N-protected building blocks in each step, we have investigated an N→C extension route that is based on activation of a peptide C-terminal amide protecting group to the corresponding methyl ester. We found that this conversion is efficiently catalysed by Stenotrophomonas maltophilia peptide amidase in neat organic media. The system excludes the possibility of internal peptide cleavage as the enzyme lacks intrinsic protease activity. The produced peptide methyl ester was used for peptide chain extension in a kinetically controlled reaction by a thermostable protease.

Modular construction of quaternary hemiaminal-based inhibitor candidates and their in cellulo assessment with HIV-1 protease

Non-peptidomimetic drug-like protease inhibitors have potential for circumventing drug resistance. We developed a much-improved synthetic route to our previously reported inhibitor candidate displaying an unusual quaternized hemi-aminal. This functional group forms from a linear precursor upon passage into physiological media. Seven variants were prepared and tested in cellulo with our HIV-1 fusion-protein technology that result in an eGFP-based fluorescent readout. Three candidates showed inhibition potency above 20 μM and toxicity at higher concentrations, making them attractive targets for further refinement. Importantly, our class of original inhibitor candidates is not recognized by two major multidrug resistance pumps, quite in contrast to most clinically applied HIV-1 protease inhibitors.

New β-strand templates constrained by Huisgen cycloaddition

New peptidic templates constrained into a β-strand geometry by linking acetylene and azide containing P1 and P3 residues of a tripeptide by Huisgen cycloaddition are presented. The conformations of the macrocycles are defined by NMR studies and those that best define a β-strand are shown to be potent inhibitors of the protease calpain. The β-strand templates presented and defined here are prepared under optimized conditions that should be suitable for targeting a range of proteases and other applications requiring such a geometry.

METHODS AND SYSTEMS FOR PREPARING IRREVERSIBLE INHIBITORS OF PROTEIN TYROSINE PHOSPHATASES

Described herein are the preparation and use of novel bromo- phosphonomethylphenylalanine amino acid derivatives (BrPmp) and BrPmp-containing peptides as specific, irreversible protein tyrosine phosphatase inhibitors, which are suitable for application in peptide synthesis. These derivatives are particularly advantageous since their synthesis is both easy and scalable, and they are suitable for peptide synthesis. The BrPmp derivatives described herein can be appropriately protected to allow for solid phase peptide synthesis (SPPS) and incorporation into peptides for preparation of protein tyrosine phosphatase inhibitors and inhibitor libraries. The peptides and peptide libraries can be used to identify new protein tyrosine phosphatase specific sequences and profile protein tyrosine phosphatase activity in cell lysates, diagnostic samples and biopsy samples.