121343-82-6

Basic information

• Product Name: Fmoc-L-glutamic acid
• Synonyms: N-Fmoc-L-glutamic Acid Fmoc-Glu-OH;(S)-2-((((9H-Fluoren-9-yl)Methoxy)carbonyl)aMino)pentanedioic acid;Fmoc-Glu;Fmoc-L-glutamic acid≥ 98% (HPLC);FMOC-GLU-OH;FMOC-GLUTAMIC ACID;FMOC-L-GLUTAMIC ACID;FMOC-L-GLU-OH
• CAS NO: 121343-82-6
• Molecular Formula: C₂₀H₁₉NO₆
• Molecular Weight: 369.37
• Product Categories: Amino Acids;Glutamic acid [Glu, E];Fmoc-Amino Acids and Derivatives;Amino Acids (N-Protected);Biochemistry;Fmoc-Amino Acids;Fmoc-Amino acid series
• Mol File: 121343-82-6.mol

Chemical Properties

• Boiling Point: 635.8 °C at 760 mmHg
• Flash Point: 338.3 °C
• Appearance: /
• Density: 1.366 g/cm³
• Vapor Pressure: 4.89E-17mmHg at 25°C
• Refractive Index: 1.618
• Storage Temp.: Store at RT.
• PKA: 3.72±0.10(Predicted)
• Water Solubility: Slightly soluble in water.
• CAS DataBase Reference: Fmoc-L-glutamic acid(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-L-glutamic acid(121343-82-6)
• EPA Substance Registry System: Fmoc-L-glutamic acid(121343-82-6)

Safety Data

• Safety Statements: 24/25
• Hazardous Substances Data: 121343-82-6(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Fmoc-L-glutamic acid is used as a therapeutic agent for patients who have liver disease accompanied by encephalopathy, a condition also known as hepatic coma. Its role in the central nervous system and as a neurotransmitter makes it a valuable compound for treating this specific health condition.
Used in Research and Development:
Fmoc-L-glutamic acid is utilized as a key component in the synthesis of various peptides and pharmaceuticals due to its unique properties as a nonessential amino acid. Its presence in the synthesis process aids in the development of new drugs and therapies targeting the central nervous system and other related conditions.

InChI:InChI=1/C20H19NO6/c22-18(23)10-9-17(19(24)25)21-20(26)27-11-16-14-7-3-1-5-12(14)13-6-2-4-8-15(13)16/h1-8,16-17H,9-11H2,(H,21,26)(H,22,23)(H,24,25)/t17-/m0/s1

Upstream product

• 56-86-0 L-glutamic acid 
• 1131148-55-4 1-[(9-fluorenylmethyloxycarbonyl)]benzotriazole 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 84418-43-9 9-fluorenylmethyl carbamate 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 84793-07-7 Fmoc-Glu-OtBu 
• 71989-18-9 Fmoc-Glu(OtBu)-OH 
• 1481642-14-1 (S)-4-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-5-methoxy-5-oxopentanoic acid 

Downstream Products

• 129460-14-6 N-(9-fluorenylmethoxycarbonyl)glutamic acid di-tert-butyl ester 

Relevant articles and documents

SUPRAMOLECULAR GEL SUPPORTED ON OPEN-CELL POLYMER FOAM

The present invention relates to a polymer foam, said polymer foam comprising pores forming an open-cell polymer foam, said polymer foam comprising a supramolecular gel inside pores, and said polymer foam comprising at least one enzyme. The present invention relates to a supramolecular gel; its preparation and its applications, notably in chemical synthesis and kinetic resolution, in particular of organic compounds. The present invention also relates to flow chemistry.

Preparation method of N-fluorenylmethoxycarbonyl-gamma-(S-triphenylmethyl-cysteamine)-L-glutamic acid

The invention provides a preparation method of N-fluorenylmethoxycarbonyl-gamma-(S-triphenylmethyl-cysteamine)-L-glutamic acid. The preparation method mainly solves the technical problems of complexity, long period, high cost, and low yield of an original process, and comprises the following steps: (1) preparing N-fluorenylmethoxycarbonyl-L-glutamic acid; (2) preparing N-fluorenylmethoxycarbonyl-L-glutamic acid-1-benzyl ester; (3) preparing S-triphenylmethyl cysteamine; (4) preparing N-fluorenylmethoxycarbonyl-gamma-(S-triphenylmethyl-cysteamine)-L-glutamic acid-alpha-benzyl ester; and (5) preparing N-fluorenylmethoxycarbonyl-gamma-(S-triphenylmethyl-cysteamine)-L-glutamic acid. The method is rapid, high in yield and simple in separation and purification, and the used solvent is environment-friendly and is suitable for mass production.

Supported Catalytically Active Supramolecular Hydrogels for Continuous Flow Chemistry

Inspired by biology, one current goal in supramolecular chemistry is to control the emergence of new functionalities arising from the self-assembly of molecules. In particular, some peptides can self-assemble and generate exceptionally catalytically active fibrous networks able to underpin hydrogels. Unfortunately, the mechanical fragility of these materials is incompatible with process developments, relaying this exciting field to academic curiosity. Here, we show that this drawback can be circumvented by enzyme-assisted self-assembly of peptides initiated at the walls of a supporting porous material. We applied this strategy to grow an esterase-like catalytically active supramolecular hydrogel (CASH) in an open-cell polymer foam, filling the whole interior space. Our supported CASH material is highly efficient towards inactivated esters and enables the kinetic resolution of racemates. This hybrid material is robust enough to be used in continuous flow reactors, and is reusable and stable over months.

Molecular Scaffolds as Double-Targeting Agents For the Diagnosis and Treatment of Neuroblastoma

The selective delivery of therapeutic and imaging agents to tumoral cells has been postulated as one of the most important challenges in the nanomedicine field. Meta-iodobenzilguanidine (MIBG) is widely used for the diagnosis of neuroblastoma (NB) due to its strong affinity for the norepinephrine transporter (NET), usually overexpressed on the membrane of malignant cells. Herein, a family of novel Y-shaped scaffolds has been synthesized, which have structural analogues of MIBG covalently attached at each end of the Y-structure. The cellular uptake capacity of these double-targeting ligands has been evaluated in vitro and in vivo, yielding one specific Y-shaped structure that is able to be engulfed by the malignant cells, and accumulates in the tumoral tissue, at significantly higher levels than the structure containing only one single targeting agent. This Y-shaped ligand can provide a powerful tool for the current treatment and diagnosis of this disease.

LIGANDS FOR ENHANCED IMAGING AND DRUG DELIVERY TO NEUROBLASTOMA CELLS

The present invention concerns aminobenzylguanidine derivative ligands specifically targeting neuroblastoma cells with an improved cellular uptake. The improved cellular uptake provides for the therapeutic and diagnostic use of the ligands in neuroblastoma-related diseases.

Fmoc-OPhth, the reagent of Fmoc protection

Fmoc-OSu has been widely used for Fmoc protection of amino groups, especially amino acids, in solid phase peptide synthesis. However, it has been recognized that Fmoc-βAla-OH is formed as a by-product via the Lossen rearrangement during the reaction. Since we reconfirmed the formation of Fmoc-βAla-OH during the preparation of Fmoc-AA-OH by Fmoc-OSu, Fmoc-OPhth was designed and synthesized as a new Fmoc reagent to avoid the formation of Fmoc-βAla-OH. Furthermore, Fmoc protection by Fmoc-OPhth and Fmoc-SPPS were evaluated. The various Fmoc-amino acids prepared by Fmoc-OPhth were carried out in good yields and these are applicable in Fmoc-SPPS.

New TFA-free cleavage and final deprotection in Fmoc solid-phase peptide synthesis: Dilute HCl in fluoro alcohol

A novel method for cleaving from resin and removing acid-labile protecting groups for the Fmoc solid-phase peptide synthesis is described. 0.1 N HCl in hexafluoroisopropanol or trifluoroethanol cleanly and rapidly removes the tert-butyl ester and ether, Boc, trityl, and Pbf groups and cleaves the common resin linkers: Wang, HMPA, Rink amide, and PAL. Addition of just 5-10% of a hydrogen-bonding solvent considerably retards or even fully inhibits the reaction. However, a non-hydrogen-bonding solvent is tolerated.

Liquid-chromatography quantitative analysis of 20 amino acids after derivatization with FMOC-CI and its application to different origin Radix isatidis

We developed a simple, rapid and reliable method for determination of 20 common amino acids based on derivatization with 9-fluorenylmethyl chloroformate (FMOC-CI) and RP-LC/UV, this method was first introduced into quantitative analysis of amino acids. The amino groups of amino acids were trapped with FMOC-CI to form amino acid-FMOC-Cl adducts which can be suitable for LC-UV. Chromatographic separation was performed on a C18 column with a mobile phase gradient consisting of acetonitrile and sodium acetate solution. This method was shown to be sensitive for 20 common amino acids. In the intra-day precisions assay, the range of RSDs was 3.21-7.67% with accuracies of 92.34-102.51%; for the inter-day precisions assay, the range of RSDs was 5.82-9.19% with accuracies of 90.25-100.63%. The results also indicated that solutions of amino acids-FMOC-Cl can be kept at room temperature for at least 24 h without showing significant losses in the quantified values. The validated method was successfully applied to the determination of major four kinds of amino acids in R. isatidis samples (Arg, Pro, Met and Val). The total content of amino acids in different origin R. isatidis was 13.32-19.16 mg/g. The differences between R. isatidis samples were large using HCA.

Multicomponent hydrogels from enantiomeric amino acid derivatives: Helical nanofibers, handedness and self-sorting

In this study, chiral helical nanofibers have been obtained from suitable, co-assembling, two oppositely charged amino acid based two component hydrogels. An equimolar mixture of an N-terminally protected amino acid Fmoc-(l/d)Glu (Fmoc: N-fluorenyl-9-methoxycarbonyl, Glu: glutamic acid) and (l/d)Lys (Lys: lysine) can co-assemble to form hydrogels. These hydrogels have been characterised using circular dichroism (CD), atomic force microscopy (AFM), transmission electron microscopy (TEM), X-ray powder diffraction, fluorescence spectroscopic and rheological studies. CD and AFM studies have been extensively used to examine the chiral/achiral nature of fibers obtained from different hydrogel systems. The equimolar mixture of two l-isomers, {Fmoc-(l)Glu + (l)Lys} in the assembled state, leads to the exclusive formation of left-handed helical nanofibers, whereas an equimolar mixture of two d-isomers, {Fmoc-(d)Glu + (d)Lys}, gives rise to right-handed helical nanofibers. The CD study of the gel obtained from the {Fmoc-(l)Glu + (l)Lys} system is exactly the mirror image of the CD signal obtained from the gel of the {Fmoc-(d)Glu + (d)Lys} system. These results suggest that the molecular chirality is being translated into the supramolecular helicity and the handedness of these fibers depends on the corresponding molecular chirality in the mixture of the two component system. Reversing the handedness of helical fibers is possible by using enantiomeric building blocks. Co-assembly of racemic and equimolar mixtures of all four components, i.e., [{Fmoc-(l)Glu + (l)Lys} + {Fmoc-(d)Glu + (d)Lys}] can also form hydrogels. Interestingly, in this racemic mixture self-sorting has been observed with the presence of almost equal amount of left- and right-handed helical nanofibers. The equimolar mixture of Fmoc-(l)Glu and l-ornithine/l-arginine also produces hydrogel with left-handed helical fibers. Moreover, the straight fiber has been observed from the two component hydrogel {Fmoc-(l)Glu + (l)Lys} system in the presence of Ca2+/Mg2+ ions. This indicates the straight nanofibers are obtained under suitable conditions and acid-base interaction is responsible for making the helical fibers at the nanoscale.

Benzotriazole reagents for the syntheses of Fmoc-, Boc-, and Alloc-protected amino acids

Stable Fmoc-, Boc-, and Alloc-benzotriazoles react with various amino acids including unprotected serine and glutamic acid, in the presence of triethylamine at 20° as reagents to introduce -amino protecting groups to afford Fmoc-, Boc-, and Alloc-protected amino acids (77-94%) free of dipeptide and tripeptide impurities. Fmoc-, and Alloc-Gly-Gly-OH dipeptides were prepared in 90% yields by N-acylation of glycylglycine with Fmoc- and Alloc-benzotriazoles in the presence of triethylamine. Synthesized N-protected amino acids were greater than 99% pure, analyzed by HPLC. Georg Thieme Verlag Stuttgart - New York.