82911-79-3

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

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

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 
• 132409-94-0 N-(9-Fluorenylmethoxycarbonyl)-O-tert-butyl-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 

Relevant academic research and scientific papers

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.

Macrocyclic peptide inhibitors of serine proteases. Convergent total synthesis of cyclotheonamides A and B via a late-stage primary amine intermediate. Study of thrombin inhibition under diverse conditions

Cyclotheonamide A (CtA, 1), a cyclic pentapeptide isolated from the marine sponge Theonella sp., is an inhibitor of serine proteases such as α-thrombin and trypsin. We describe, in detail, our total synthesis of CtA by a convergent [3 + 2] fragment-conden

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.