35661-40-6

Basic information

• Product Name: FMOC-L-Phenylalanine
• Synonyms: FMOC-L-PHE;FMOC-L-PHENYLALANINE;FMOC-L-PHE-OH;9-FLUORENYLMETHOXYCARBONYL-L-PHENYLALANINE;N-(9-FLUORENYLMETHOXYCARBONYL)-L-PHENYLALANINE;N-9-FLUORENYLMETHYLOXYCARBONYL-L-PHENYLALANINE;N-[(9H-FLUOREN-9-YLMETHOXY)CARBONYL]-L-PHENYLALANINE;N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-L-PHENYLALANINE
• CAS NO: 35661-40-6
• Molecular Formula: C₂₄H₂₁NO₄
• Molecular Weight: 387.43
• EINECS: 252-661-1
• Product Categories: Protected Amino Acids;Fluorenes, Flurenones;Amino Acids;Phenylalanine [Phe, F];Fmoc-Amino Acids and Derivatives;Amino Acids (N-Protected);Biochemistry;Fmoc-Amino Acids;Fmoc-Amino acid series;A;Benzopyrans
• Mol File: 35661-40-6.mol

Chemical Properties

• Melting Point: 180-187 °C(lit.)
• Boiling Point: 513.39°C (rough estimate)
• Flash Point: 328.8 °C
• Appearance: White/Powder
• Density: 1.2379 (rough estimate)
• Vapor Pressure: 3.07E-16mmHg at 25°C
• Refractive Index: -39.5 ° (C=1, DMF)
• Storage Temp.: 2-8°C
• Solubility: Chloroform (Slightly), DMF (Sparingly, Sonicated), DMSO (Slightly)
• PKA: 3.77±0.10(Predicted)
• BRN: 3597808
• CAS DataBase Reference: FMOC-L-Phenylalanine(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-L-Phenylalanine(35661-40-6)
• EPA Substance Registry System: FMOC-L-Phenylalanine(35661-40-6)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 22-24/25-26
• WGK Germany: 3
• Hazardous Substances Data: 35661-40-6(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
FMOC-L-Phenylalanine is used as a building block for the synthesis of peptides and peptide-based drugs. Its incorporation into peptide structures allows for the development of novel therapeutic agents with specific biological activities.
Used in Research and Development:
FMOC-L-Phenylalanine serves as a valuable tool in the research and development of new drugs and therapies. It is used in the preparation of deltorphin derivatives, which are known for their potent analgesic properties. This amino acid derivative can also be utilized in the study of the IGF-I and IGF-Binding Protein-5 complex, potentially leading to the development of treatments for conditions related to these proteins.
Used in Chemical Synthesis:
As a chemical intermediate, FMOC-L-Phenylalanine is used in the synthesis of various compounds with specific functional groups. Its reactivity and structural properties make it a versatile building block for creating complex molecules with tailored properties for different applications.

InChI:InChI=1/C24H21NO4/c26-23(27)22(14-16-8-2-1-3-9-16)25-24(28)29-15-21-19-12-6-4-10-17(19)18-11-5-7-13-20(18)21/h1-13,21-22H,14-15H2,(H,25,28)(H,26,27)/p-1/t22-/m0/s1

Upstream product

• 63-91-2 L-phenylalanine 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 100821-63-4 1,2,2,2-Tetrachloroethyl 9-fluorenylmethyl carbonate 
• 100803-85-8 3-(9-Fluorenylmethoxycarbonyl)-benzoxazoline-2-thione 
• 88744-04-1 (9-fluorenyl)methyl pentafluorophenyl carbonate 
• 99503-04-5 Carbonic acid 3,5-dioxo-4-aza-tricyclo[5.2.1.0^2,6]dec-8-en-4-yl ester 9H-fluoren-9-ylmethyl ester 
• 146549-19-1 (2S)-N-<(fluoren-9-yl)methoxycarbonyl>phenylalanine prop-2-enyl ester 
• 129460-18-0 Fmoc-Phe-O-t-Bu 
• 394210-45-8 4-benzyl-2,5-dioxo-oxazolidine-3-carboxylic acid 9H-fluoren-9-ylmethyl ester 
• 548740-17-6 2-[3,5-bis(trifluoromethyl)phenylsulfonyl]ethyl N-(9-fluorenylmethyloxycarbonyl)phenylalanine 
• 129397-83-7 (9-fluorenylmethoxycarbonyl)-L-phenylalaninol 
• 129397-81-5 methyl (((9H-fluoren-9-yl)methoxy)carbonyl)-L-phenylalaninate 
• 246158-11-2 tert-butyl [(1S,2S)-2-azido-3-(4-tert-butoxyphenyl)-1-(2-oxoethyl)propoxy]acetate 

Downstream Products

• 101214-43-1 Fmoc-Phe-ONSu 
• 84000-03-3 9H-fluoren-9-ylmethyl (S)-4-benzyl-5-oxo-1,3-oxazolidine-3-carboxylate 
• 71989-30-5 Fmoc-Phe-ONp 
• 113534-35-3 Fmoc-Phe-OTDO 
• 86060-92-6 N-α-Fmoc-L-phenylalanine pentafluorophenyl ester 
• 82068-55-1 Ava-Phe-Phe-Gly-Leu-Met-NH₂ 
• 127492-89-1 Ava-Phe-Phe-Pro-Leu-Met-NH₂ 
• 127492-90-4 Ava-Phe-Phe-D-Pro-Leu-Met-NH₂ 
• 87720-56-7 t-butyl-N-fluoren-9-ylmethyloxycarbonyl-L-phenylalanyl-O-t-butyl-L-threonine 
• 110172-15-1 H-Tyr-Orn[*]-Phe-Asp[*]-NH₂ 
• 110116-75-1 H-Tyr-D-Asp[*]-Phe-A₂bu[*]-NH₂ 
• 106818-61-5 H-Tyr-D-Orn[*]-Phe-D-Asp[*]-NH₂ 
• 127633-31-2 Fmoc-Phe-benzotriazolyl ester 
• 146803-37-4 N-(fluorenylmethyloxycarbonyl)-L-phenylalanine S-benzyl thioester 

Relevant articles and documents

A combined SPS-LCD sensor for screening protease specificity

A hydrogel-based sensor for screening protease specificity has been developed that combines the versatility of solid-phase synthesis (SPS) with the simplicity of liquid crystal display (LCD) technology. The Royal Society of Chemistry.

Single Amino-Acid Based Self-Assembled Biomaterials with Potent Antimicrobial Activity

The design and development of soft biomaterials based on amino acid and short-peptide have gained much attention due to their potent biomedical applications. A slight alteration in the side-chain of single amino acid in a peptide or protein sequence has a huge impact on the structure and function. Phenylalanine is one of the most studied amino acids, which contains an aromatic phenyl group connected through a flexible ?CH2? unit. In this work, we have examined whether flexibility and aromatic functionality of phenylalanine (Phe) are important in gel formation of model gelator Fmoc-Phe-OH or not. To examine this hypothesis, we synthesized Fmoc-derivatives of three analogues unnatural amino acids including cyclohexylalanine, phenylglycine, and homophenylalanine; which are slightly varied from Phe. Interestingly, all these three new analogues formed hydrogels in phosphate buffer at pH 7.0 having different gelation efficacy and kinetics. This study suggests that the presence of aromatic side-chain and flexibility are not mandatory for the gelation of this model gelator. Newly synthesized unnatural amino acid derivatives have also exhibited promising antimicrobial activity towards gram-positive bacteria by inhibiting cellular oxygen consumption. We further determined the biocompatibility of these amino acid derivatives by using a hemolysis assay on human blood cells. Overall studies described the development of single amino acid-based new injectable biomaterials with improved antimicrobial activity by the slight alteration in the side-chain of amino acid.

Fungal Dioxygenase AsqJ Is Promiscuous and Bimodal: Substrate-Directed Formation of Quinolones versus Quinazolinones

Previous studies showed that the FeII/α-ketoglutarate dependent dioxygenase AsqJ induces a skeletal rearrangement in viridicatin biosynthesis in Aspergillus nidulans, generating a quinolone scaffold from benzo[1,4]diazepine-2,5-dione substrates. We report that AsqJ catalyzes an additional, entirely different reaction, simply by a change in substituent in the benzodiazepinedione substrate. This new mechanism is established by substrate screening, application of functional probes, and computational analysis. AsqJ excises H2CO from the heterocyclic ring structure of suitable benzo[1,4]diazepine-2,5-dione substrates to generate quinazolinones. This novel AsqJ catalysis pathway is governed by a single substituent within the complex substrate. This unique substrate-directed reactivity of AsqJ enables the targeted biocatalytic generation of either quinolones or quinazolinones, two alkaloid frameworks of exceptional biomedical relevance.

Novel chiral stationary phases based on 3,5-dimethyl phenylcarbamoylated β-cyclodextrin combining cinchona alkaloid moiety

Novel chiral selectors based on 3,5-dimethyl phenylcarbamoylated β-cyclodextrin connecting quinine (QN) or quinidine (QD) moiety were synthesized and immobilized on silica gel. Their chromatographic performances were investigated by comparing to the 3,5-dimethyl phenylcarbamoylated β-cyclodextrin (β-CD) chiral stationary phase (CSP) and 9-O-(tert-butylcarbamoyl)-QN-based CSP (QN-AX). Fmoc-protected amino acids, chiral drug cloprostenol (which has been successfully employed in veterinary medicine), and neutral chiral analytes were evaluated on CSPs, and the results showed that the novel CSPs characterized as both enantioseparation capabilities of CD-based CSP and QN/QD-based CSPs have broader application range than β-CD-based CSP or QN/QD-based CSPs. It was found that QN/QD moieties play a dominant role in the overall enantioseparation process of Fmoc-amino acids accompanied by the synergistic effect of β-CD moiety, which lead to the different enantioseparation of β-CD-QN-based CSP and β-CD-QD-based CSP. Furthermore, new CSPs retain extraordinary enantioseparation of cyclodextrin-based CSP for some neutral analytes on normal phase and even exhibit better enantioseparation than the corresponding β-CD-based CSP for certain samples.

Determination of Chemical and Enantiomeric Purity of α-Amino Acids and their Methyl Esters as N-Fluorenylmethoxycarbonyl Derivatives Using Amylose-derived Chiral Stationary Phases

Liquid chromatographic enantiomer separation and simultaneous determination of chemical and enantiomeric purity of α-amino acids and their methyl esters as N-fluorenylmethoxycarbonyl (FMOC) derivatives was performed on three covalently bonded type chiral stationary phases (CSPs) derived from amylose derivatives. The enantiomer separation of α-amino acid esters as N-FMOC derivatives was better than that of the corresponding acids, especially for CSP 1 and 2. Chemical impurities as the corresponding racemic acids present in several commercially available racemic amino acid methyl esters were observed to be 0.49–17.50%. Enantiomeric impurities of several commercially available L-amino acid methyl esters were found to be 0.03–0.58%, whereas chemical impurities as the corresponding racemic acids present in the same analytes were found to be 0.13–13.62%. This developed analytical method will be useful for the determination of chemical and enantiomeric purity of α-amino acids and/or esters as N-FMOC derivatives using amylose-derived CSPs.

Dicyclohexylurea derivatives of amino acids as dye absorbent organogels and anion sensors

Dicyclohexyl urea (DCU) derivatives of amino acids Fmoc-Phe-DCU (M1), Fmoc-Phg-DCU (M2) and Fmoc-Gaba-DCU (M3) have been shown to form phase selective, thermoreversible and mechanically robust gels in a large range of organic solvents. This is the first report of low molecular weight gelators (LMWG) from DCU derivatives of amino acids. The self-assembly mechanism of the organogels has been probed using concentration dependent 1H NMR, DMSO titration 1H NMR, fluorescence, FTIR, PXRD and FESEM techniques. Self-assembly leading to gelation process is mainly driven by hydrophobicity and π-π stacking interactions in between Fmoc groups. Interestingly, the gels can absorb several kinds of organic dyes efficiently and can be reused for dye absorption for multiple cycles. Additionally, M1-M3 act as sensors for anions like fluoride, acetate and hydroxide, for which they have specific fluorescence response. Gel formation by M1-M3 is completely arrested in the presence of fluoride. The possible binding mode of fluoride has been delineated using DFT studies. Calculations suggest, involvement of urea NH in a six membered intramolecular hydrogen bond, rendering it unavailable for fluoride binding. Backbone -NH of the amino acids of M1-M3 is responsible for fluoride binding. The reported small, economically viable, synthetically facile molecules not only enrich the repertoire of LMWG molecules, but can have multifaceted applications.

Evaluation of the Edman degradation product of vancomycin bonded to core-shell particles as a new HPLC chiral stationary phase

A modified macrocyclic glycopeptide-based chiral stationary phase (CSP), prepared via Edman degradation of vancomycin, was evaluated as a chiral selector for the first time. Its applicability was compared with other macrocyclic glycopeptide-based CSPs: TeicoShell and VancoShell. In addition, another modified macrocyclic glycopeptide-based CSP, NicoShell, was further examined. Initial evaluation was focused on the complementary behavior with these glycopeptides. A screening procedure was used based on previous work for the enantiomeric separation of 50 chiral compounds including amino acids, pesticides, stimulants, and a variety of pharmaceuticals. Fast and efficient chiral separations resulted by using superficially porous (core-shell) particle supports. Overall, the vancomycin Edman degradation product (EDP) resembled TeicoShell with high enantioselectivity for acidic compounds in the polar ionic mode. The simultaneous enantiomeric separation of 5 racemic profens using liquid chromatography-mass spectrometry with EDP was performed in approximately 3?minutes. Other highlights include simultaneous liquid chromatography separations of rac-amphetamine and rac-methamphetamine with VancoShell, rac-pseudoephedrine and rac-ephedrine with NicoShell, and rac-dichlorprop and rac-haloxyfop with TeicoShell.

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.

Fmoc-Amox, A Suitable Reagent for the Introduction of Fmoc

Synthesis of most peptides is achieved using solid-phase peptide synthesis employing the Fmoc/tert-butyl strategy. However, the introduction of Fmoc in N-unprotected amino acids seems to be challenging due to the formation of dipeptides and sometimes tripeptides as impurities and β-alanyl impurities when Fmoc-OSu is used as well. Herein, we report an efficient and successful method using Fmoc-Amox, which is an oxime based derivative, toward the synthesis of Fmoc-glycine with no traces of side reactions. Fmoc-Amox is inexpensive, and Amox can be easily removed after the reaction, thus affording pure Fmoc-Gly-OH devoid of any detrimental impurities or contamination, mainly dipeptide or Amox itself, as shown by high-performance liquid chromatography and NMR, respectively.

Synthesis and biological evaluation of novel FK228 analogues as potential isoform selective HDAC inhibitors

Novel C4- and C7-modified FK228 analogues were efficiently synthesized in a highly convergent and unified manner. This synthesis features the amide condensation of glycine-d-cysteine-containing segments with d-valine-containing segments for the direct assembly of the corresponding seco-acids, which are key precursors of macrolactones. The HDAC inhibition assay and cell-growth inhibition analysis of the synthesized analogues revealed novel aspects of their structure-activity relationship. This study demonstrated that simple modification at the C4 and C7 side chains in FK228 is effective for improving both HDAC inhibitory activity and isoform selectivity; moreover, potent and highly isoform-selective class I HDAC1 inhibitors were identified.