102410-65-1

Basic information

• Product Name: Fmoc-L-phenylglycine
• Synonyms: [(9H-Fluoren-9-ylmethoxycarbonylamino)]phenylacetic acid;FMoc-Phg-OH FMoc-L-phenylglycine;N-Fmoc-L-2-phenylglycine Fmoc-Phg-OH;(S)-2-((((9H-Fluoren-9-yl)Methoxy)carbonyl)aMino)-2-phenylacetic acid;N-FMoc-L-^a-phenylglycine, 98%;FMoc-(S)-phenylglycine;FMoc-Phg-OH, >=98.0%;(S)-Fmoc-2-aminophenylacetic acid
• CAS NO: 102410-65-1
• Molecular Formula: C₂₃H₁₉NO₄
• Molecular Weight: 373.4
• EINECS: 1533716-785-6
• Product Categories: Fmoc-Amino acid series;Amino Acids;Phenylglycine [Phg];Unusual Amino Acids;Amino Acids (N-Protected);Biochemistry;Fmoc-Amino Acids
• Mol File: 102410-65-1.mol

Chemical Properties

• Melting Point: 175-180 °C
• Boiling Point: 606.3 °C at 760 mmHg
• Flash Point: 320.5 °C
• Appearance: /Solid
• Density: 1.299 g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 81 ° (C=1, DMF)
• Storage Temp.: 2-8°C
• Solubility: soluble in Methanol
• PKA: 3.39±0.10(Predicted)
• BRN: 5309005
• CAS DataBase Reference: Fmoc-L-phenylglycine(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-L-phenylglycine(102410-65-1)
• EPA Substance Registry System: Fmoc-L-phenylglycine(102410-65-1)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• F: 10
• HazardClass: IRRITANT
• Hazardous Substances Data: 102410-65-1(Hazardous Substances Data)

Usage

Chemical Properties

Solid

InChI:InChI=1/C23H19NO4/c25-22(26)13-15-6-5-7-16(12-15)24-23(27)28-14-21-19-10-3-1-8-17(19)18-9-2-4-11-20(18)21/h1-12,21H,13-14H2,(H,24,27)(H,25,26)

Upstream product

• 102410-51-5 H-D-Abu-Pro-OBu^t*TosOH 
• 102419-78-3 Pic(3-OBzl)-Thr(Fmoc-Phg-)-N₂H₃*2*HCl 
• 2935-35-5 (S)-2-phenylglycine 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 2835-06-5 phenylglycin 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 163883-97-4 2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-2-phenylacetic acid 
• 69-91-0 L-α-phenylglycine 

Downstream Products

• 110116-73-9 H-Tyr-D-Orn<*>-Phg-Asp<*>-NH2 
• 102410-54-8 Pic(3-OBzl)-Thr(Fmoc-Phg-)-NHNH-Boc 
• 396091-74-0 H-Phe-(2S,4R)-(4-OCO-NH-CH₂-CH₂-NH-Boc)-Pro-Phg-D-Trp(Boc)-Lys(Boc)-Tyr(Bzl)-OH 
• 839719-68-5 pentafluorophenyl L-α-[(9H-fluoren-9-ylmethoxycarbonyl)amino]-α-benzeneethanoate 

Relevant articles and documents

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.

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.

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.

IMMUNE CELL MODULATORS

Disclosed are immune cell-selective small molecule compounds that modulate certain immune cell-specific receptors and enzymes, and methods of their synthesis and use to treat proliferative disorders.

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.

A SYNTHETIC CYCLIC DIPEPTIDE AND A PROCESS THEREOF

The disclosure relates to preparation and self-assembly of aromatic cyclic dipeptide into one and two dimensional nano, meso and micro structures. The said structures of cyclic dipeptide can be electrospinned into threads, fabrics, suture, bandage materials. They are also useful in cell culturing, tissue culturing, drug delivery system, as composite materials, as inhibitors of fibrillization and in Biomedical research such as neurological regeneration and organ replacement studies.

Efficient procedure for the preparation of oligomer-free N-fmoc amino acids

A two-step method is presented for the peptide-free, high-purity, and high-yield synthesis of N-Fmoc amino acids. The first step involves the preparation of stable dicyclohexylammonium-amino acid ionic adduct in acetone. Subsequently, the ionic adducts, on reaction with Fmoc-Nosu under mild alkaline conditions, give dipeptide-free N-Fmoc amino acids. The positive charge of the dicyclohexylammonium counterion in the ionic salt has a longer radius, moderating the nucleophilicity of the carboxylate ion of the amino acid and preventing by-products by arresting the formation of mixed anhydrides, the precursors of oligopeptide impurities.

Site-specific incorporation of non-natural residues into peptides: Effect of residue structure on suppression and translation efficiencies

A systematic survey of the structural requirements for biosynthetic incorporation of non-natural residues into a polypeptide is presented. Relative translation efficiencies for a series of 12 semi-synthetic acylated suppressor tRNAs ranged from 0 to 91% depending on the structure of the residue incorporated.

SIMULTANEOUS USE OF N-Fmoc AND OTmse PROTECTIVE GROUPS IN THE SYNTHESIS OF PEPTOLYTIC SENSITIVE PEPTIDES

The combined use of Fmoc (fluorenylmethoxycarbonyl) as N-protection and Tmse (trimethylsilylethyl) as O-protection during demanding fragment condensation mediated by Bop-Cl (N,N'-bis(3-oxo-2-oxazolidinyl)phosphinyl chloride) has been explored in the preparation of useful synthons that are sensitive to acidic and even basic hydrolyses.Stepwise deprotection by morfoline (Fmoc-deprotection) followed by F--mediated removal of Tmse results in a very effective peptide synthesis strategy, as exemplified by the preparation of i.a.Phg-MePhe-Thz.Similarly, combinations of N-Boc, O-Tmse peptide esters are also possible that allow the preparation of +H2-MePhe-Thz-OTmse (via Boc-MePhe-Thz-OTmse) without competitive DKP formation.