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
• Article Data: 13

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

General Description

FMOC-TYR-OME is a chemical compound commonly used in the field of organic chemistry. It is derived from the amino acid tyrosine and is often used as a building block in the synthesis of peptides. FMOC-TYR-OME is used as a protecting group for the tyrosine residue, allowing for selective modification of other amino acids within the peptide chain. FMOC-TYR-OME is widely used in laboratory settings for peptide synthesis and has applications in the development of pharmaceuticals, as well as in the study of protein structure and function.

Upstream product

• 1080-06-4 L-Tyr-OMe 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 3417-91-2 L-tyrosine methyl ester HCl 
• 845786-39-2 3-{4-[2-(tert-butyl-diphenyl-silanyl)-ethoxy]-phenyl}-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionic acid methyl ester 
• 24324-17-2 9-Fluorenylmethanol 
• 82911-72-6 dicyclohexylamine salt of N-hydroxysuccinimide 
• 101-83-7 N-cyclohexyl-cyclohexanamine 
• 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 

Downstream Products

• 168135-78-2 methyl N^α-Fmoc-4-O-tyrosinate 
• 298693-92-2 N-(fluorenyl-9-methoxycarbonyl)-L-O-trifluoromethylsulfonyl-tyrosine methyl ester 
• 1099718-55-4 N-(9-fluorenylmethoxycarbonyl)-O'-phosphonotyrosine methyl ester 
• 1240497-07-7 N-(9-fluorenylmehoxycarbonyl)-O-trityl-L-tyrosine methyl ester 
• 441330-34-3 C₂₆H₂₂ClNO₆ 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 
• 35068-04-3 methyl (S)-2-acetamido-3-(4-acetoxyphenyl)propanoate 
• 206060-45-9 N-(fluorenyl-9-methoxycarbonyl)-L-(p-sulfomethyl)phenylalanine 
• 945245-47-6 N-(fluorenyl-9-methoxycarbonyl)-L-(p-sulfomethyl)phenylalanine methyl ester 
• 945245-46-5 N-(fluorenyl-9-methoxycarbonyl)-L-(p-bromomethyl)phenylalanine methyl ester 

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.

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.

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.