82911-79-3

Basic information

• Product Name: FMOC-TYR-OME
• Synonyms: FMOC-TYR-OME;METHYL D-AMINOLEVULINATE HYDROCHLORIDE;(S)-Methyl 2-((((9H-fluoren-9-yl)Methoxy)carbonyl)aMino)-3-(4-hydroxyphenyl)propanoate;N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-L-tyrosine methyl ester;Fmoc-L-Tyr-OMe;N-Fmoc-L-tyrosine methyl ester;(9H-Fluoren-9-yl)MethOxy]Carbonyl Tyr-OMe
• CAS NO: 82911-79-3
• Molecular Formula: C₂₅H₂₃NO₅
• Molecular Weight: 417.45
• Mol File: 82911-79-3.mol

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: FMOC-TYR-OME(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-TYR-OME(82911-79-3)
• EPA Substance Registry System: FMOC-TYR-OME(82911-79-3)

Safety Data

• Hazardous Substances Data: 82911-79-3(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Development:
FMOC-TYR-OME is used as a building block in the synthesis of peptides for the development of pharmaceuticals. Its role as a protecting group for the tyrosine residue allows for the selective modification of other amino acids within the peptide chain, facilitating the creation of novel and effective drug candidates.
Used in Peptide Synthesis:
In the field of organic chemistry, FMOC-TYR-OME is used as a key component in peptide synthesis. Its protective function for the tyrosine residue enables chemists to selectively modify other amino acids, leading to the formation of diverse peptide sequences with specific biological activities.
Used in Protein Structure and Function Studies:
FMOC-TYR-OME is employed in laboratory settings for the study of protein structure and function. Its use in peptide synthesis allows researchers to create and modify peptides with specific tyrosine residues, enabling the investigation of their roles in protein folding, stability, and interactions with other biomolecules.

Upstream product

• 1080-06-4 L-Tyr-OMe 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 3417-91-2 L-tyrosine methyl ester HCl 
• 24324-17-2 9-Fluorenylmethanol 
• 82911-72-6 dicyclohexylamine salt of N-hydroxysuccinimide 
• 1099718-55-4 N-(9-fluorenylmethoxycarbonyl)-O'-phosphonotyrosine methyl ester 
• 186581-53-3 diazomethane 
• 112883-29-1 N-Fmoc-Tyr-OH 
• 77-78-1 dimethyl sulfate 
• 101-83-7 N-cyclohexyl-cyclohexanamine 
• 845786-39-2 3-{4-[2-(tert-butyl-diphenyl-silanyl)-ethoxy]-phenyl}-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionic acid methyl ester 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 

Downstream Products

• 168135-78-2 methyl N^α-Fmoc-4-O-tyrosinate 
• 1080-06-4 L-Tyr-OMe 
• 112883-29-1 N-Fmoc-Tyr-OH 
• 298693-92-2 N-(fluorenyl-9-methoxycarbonyl)-L-O-trifluoromethylsulfonyl-tyrosine methyl ester 
• 168135-77-1 N^α-Fmoc-O'-(O'',O''-di-tert-butyl-2-malonyl)tyrosine 
• 1240497-07-7 N-(9-fluorenylmehoxycarbonyl)-O-trityl-L-tyrosine methyl ester 
• 132409-94-0 N-(9-Fluorenylmethoxycarbonyl)-O-tert-butyl-L-tyrosine Methyl Ester 
• 1099718-55-4 N-(9-fluorenylmethoxycarbonyl)-O'-phosphonotyrosine methyl ester 
• 441330-34-3 C₂₆H₂₂ClNO₆ 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 

Relevant articles and documents

Aldolase Cascade Facilitated by Self-Assembled Nanotubes from Short Peptide Amphiphiles

Early evolution benefited from a complex network of reactions involving multiple C?C bond forming and breaking events that were critical for primitive metabolism. Nature gradually chose highly evolved and complex enzymes such as lyases to efficiently facilitate C?C bond formation and cleavage with remarkable substrate selectivity. Reported here is a lipidated short peptide which accesses a homogenous nanotubular morphology to efficiently catalyze C?C bond cleavage and formation. This system shows morphology-dependent catalytic rates, suggesting the formation of a binding pocket and registered enhancements in the presence of the hydrogen-bond donor tyrosine, which is exploited by extant aldolases. These assemblies showed excellent substrate selectivity and templated the formation of a specific adduct from a pool of possible adducts. The ability to catalyze metabolically relevant cascade transformations suggests the importance of such systems in early evolution.

Optically Pure, Structural, and Fluorescent Analogues of a Dimeric Y4 Receptor Agonist Derived by an Olefin Metathesis Approach

The dimeric peptide 1 (BVD-74D, as a diastereomeric mixture) is a potent and selective neuropeptide Y Y4 receptor agonist. It represents a valuable candidate in developing traceable ligands for pharmacological studies of Y4 receptors

Synthesis of chlorophyll-amino acid conjugates as models for modification of proteins with chromo/fluorophores

A chlorophyll-a derivative bonded directly with epoxide at the peripheral position of the chlorin π-system was reacted with N-urethane and C-ester protected amino acids bearing an alcoholic or phenolic hydroxy group as well as a carboxy group at the residue to give chlorophyll-amino acid conjugates. The carboxy residues of N,C-protected aspartic and glutamic acids were esterified with the epoxide in high yields. The synthetic conjugates in dichloromethane had absorption bands throughout the visible region including intense red-side Qy and blue-side Soret bands. By their excitation at the visible bands, strong and efficient fluorescence emission was observed up to the near-infrared region. The chromo/fluorophores are promising for preparation of functional peptides and modification of proteins.

PIPECOLIC LINKER AND ITS USE FOR CHEMISTRY ON SOLID SUPPORT

The present invention relates to a pipecolic linker and its use as a solid-phase linker in organic synthesis. Said pipecolic solid-phase linker may be used for coupling functional groups chosen between primary amines, secondary amines, aromatic amines, alcohols, phenols and thiols. In particular, said pipecolic solid-phase linker may be used for peptide or pseudopeptide synthesis, such as the reverse N to C peptide synthesis or the retro-inverso peptide synthesis, or for the synthesis of small organic molecules.

Enzyme promotes the hydrogelation from a hydrophobic small molecule

(Chemical Equation Presented) We report in this paper that an enzymatic reaction can be used as the sole mechanism for forming supramolecular hydrogels that have good stability in aqueous solutions at room temperature. The gels are two-component hydrogels that are mainly formed by hydrophobic compound 2 and doped with hydrophilic compound 1. They were formed by an enzymatic process that produces hydrophobic 2 in homogeneous modes and assists the formation of three-dimensional networks. We have characterized the morphologies of the gels with scanning electron microscopy and dark-field transmission electron microscopy, collected fluorescence data to monitor the gelation process, and proposed a possible mechanism to explain the formation of the gels.

A phosphotyrosine-imprinted polymer receptor for the recognition of tyrosine phosphorylated peptides

Hyperphosphorylation at tyrosine is commonly observed in tumor proteomes and, hence, specific phosphoproteins or phosphopeptides could serve as markers useful for cancer diagnostics and therapeutics. The analysis of such targets is, however, a challenging

tert-buyldiphenylsilylethyl ("TBDPSE"): A practical protecting group for phenols

(Chemical Equation Presented) A new protection group for phenols, the 2-(tert-butyldiphenylsilyl)ethyl (TBDPSE) group, has been prepared and investigated. Protection of a variety of substituted phenols proceeds in good to excellent yield. The group is stable to mild acid, base, hydrogenolysis conditions, and lithium/ halogen exchange on the protected phenol. Removal is achieved with strong acid or standard fluoride treatment.

Nu-alloc temporary protection in solid-phase peptide synthesis. The use of amine-borane complexes as allyl group scavengers

The use of a combination of amine-borane complexes and soluble palladium catalyst allows the fast deprotection of allyl carbamates under near-to-neutral conditions and without any side-formation of allylamine. Preliminary experiments: indicate that palladium catalyst-amine-borane systems seem ideally suited for removal of Nu-Alloc terminal groups during solid phase peptide synthesis according to the Nu-Alloc temporary protection strategy. The Royal Society of Chemistry 1999.

L-O-(2-malonyl)tyrosine (L-OMT) a new phosphotyrosyl mimic suitably protected for solidphase synthesis of signal transduction inhibitory peptides

A new phosphotyrosyl (pTyr) mimic L-O-(2-malonyl)tyrosine (L-OMT, 4) utilizes a malonyl structure in place of the parent phosphate group. This compound is stable to protein-tyrosine phosphatases and has advantages over phosphonate-based pTyr mimics in that protection of the malonyl group as its diester allows passage of the OMT across cell membranes, with subsequent esterase-mediated liberation of the free diacid once inside cells. Herein is reported the synthesis of Nα-Fmoc-L-OMT-O,O-(ferf-butyl)2 (5) for the solid-phase synthesis of L-OMT containing peptides as modulators of cellular signal transduction. Additionally included is the preparation of Nα-Fmoc-L-OMT-O,O-(n-butyl)2 (6) for the direct solid-phase synthesis of OMT-peptide diester prodrugs for use in cell-based studies.

L-O-(2-Malonyl)tyrosine: A New Phosphotyrosyl Mimetic for the Preparation of Src Homology 2 Domain Inhibitory Peptides

Inhibition of Src homology 2 (SH2) domain-binding interactions affords one potential means of modulating protein-tyrosine kinase-dependent signaling.Small phosphotyrosyl (pTyr)-containing peptides are able to bind to SH2 domains and compete with larger pTyr peptides or native pTyr-containing protein ligands.Such pTyr-containing peptides are limited in their utility as SH2 domain inhibitors in vivo due to their hydrolytic lability to protein-tyrosine phosphatases (PTPs) and the poor cellular penetration of the ionized phosphate moiety.An important aspect of SH2 domain inhibitor design is the creation of pTyr mimetics which are stable to PTPs and have reasonable bioavailability.To date, most PTP-resistant pTyr mimetics which bind to SH2 domains are phosphonates such as (phosphonomethyl)phenylalanine (Pmp, 2), phenylalanine )(FPmp, 3) or phenylalanine (F2Pmp, 4).Herein we report the incorporation of a new non-phosphorus-containing pTyr mimetic, L-O-(2-malonyl)tyrosine (L-OMT, 5), into SH2 domain inhibitory peptides using the protected analogue L-Nα-Fmoc-O'-(O'',O''-di-tert-butyl-2-malonyl)tyrosine (6) and solid-phase peptide synthesis techniques.Five OMT-containing peptides were prepared against the following SH2 domains: the PI-3 kinase C-terminal p85 SH2 domain (Ac-D-(L-OMT)-V-P-M-L-amide, 10, IC50 = 14.2 μM), the Src SH2 domain (Ac-Q-(L-OMT)-E-E-I-P-amide, 11, IC50 = 25 μM, and Ac-Q-(L-OMT)-(L-OMT)-E-I-P-amide, 14, IC50 = 23 μM), the Grb2 SH2 domain (Ac-N-(L-OMT)-V-N-I-E-amide, 12, IC50 = 120 μM), and the N-terminal SH-PTP2 SH2 domain (Ac-L-N-(L-OMT)-I-D-L-D-L-V-amide, 13, IC50 = 22.0 μM.These results show that peptides 10, 11, 13, and 14 have reasonable affinity for their respective SH2 domains, with the IC50 value for the SH-PTP2 SH2 domain-directed peptide 13 being equivalent to that previously observed for the corresponding F2Pmp-containing peptide.OMT may afford a new structural starting point for the development of novel and useful SH2 domain inhibitors.