71989-16-7

Basic information

• Product Name: Nalpha-FMOC-L-Asparagine
• Synonyms: N-ALPHA-FMOC-L-ASN;N-ALPHA-FMOC-L-ASPARAGINE;NALPHA-[(9H-FLUOREN-9-YLMETHOXY)CARBONYL]-L-ASPARAGINE;N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-N-L-ASPARAGINE;N-(9-FLUORENYLMETHOXYCARBONYL)-L-ASPARAGINE;NALPHA-(9-FLUORENYLMETHOXYCARBONYL)-L-ASPARAGINE;FMOC-ASN-OH;FMOC-ASN
• CAS NO: 71989-16-7
• Molecular Formula: C₁₉H₁₈N₂O₅
• Molecular Weight: 354.36
• EINECS: 276-252-2
• Product Categories: Fluorenes, Flurenones;Amino Acids;Asparagine [Asn, N];Fmoc-Amino Acids and Derivatives;Amino Acids (N-Protected);Biochemistry;Fmoc-Amino Acids;Fmoc-Amino acid series
• Mol File: 71989-16-7.mol

Chemical Properties

• Melting Point: 190 °C (dec.)(lit.)
• Boiling Point: 487.59°C (rough estimate)
• Flash Point: 364.2 °C
• Appearance: white to light yellow crystal powder
• Density: 1.3354 (rough estimate)
• Vapor Pressure: 2.43E-19mmHg at 25°C
• Refractive Index: -13 ° (C=1, DMF)
• Storage Temp.: 2-8°C
• PKA: 3.68±0.10(Predicted)
• BRN: 4335103
• CAS DataBase Reference: Nalpha-FMOC-L-Asparagine(CAS DataBase Reference)
• NIST Chemistry Reference: Nalpha-FMOC-L-Asparagine(71989-16-7)
• EPA Substance Registry System: Nalpha-FMOC-L-Asparagine(71989-16-7)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 24/25-36/37/39-27-26
• WGK Germany: 3
• F: 21
• HazardClass: IRRITANT
• Hazardous Substances Data: 71989-16-7(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Nalpha-FMOC-L-Asparagine is used as a building block for the synthesis of peptides and proteins, particularly in the development of targeted cancer therapies. Certain cancerous cells are known to require L-asparagine for their growth, and the N-Fmoc-protected form of this amino acid can be used to create molecules that selectively target and inhibit the growth of these cells.
Used in Chemical Synthesis:
Nalpha-FMOC-L-Asparagine is used as a protected amino acid in the synthesis of complex organic compounds and pharmaceutical agents. The N-Fmoc protection group allows for the selective incorporation of L-asparagine into peptides and other biomolecules without unwanted side reactions, ensuring the desired product is obtained with high purity and yield.
Used in Research and Development:
Nalpha-FMOC-L-Asparagine serves as an important research tool for studying the role of L-asparagine in biological processes and its potential as a therapeutic agent. Researchers can use this protected form of the amino acid to investigate its interactions with enzymes, receptors, and other biomolecules, as well as to develop new methods for its synthesis and application in medicine.

InChI:InChI=1/C19H18N2O5/c20-17(22)9-16(18(23)24)21-19(25)26-10-15-13-7-3-1-5-11(13)12-6-2-4-8-14(12)15/h1-8,15-16H,9-10H2,(H2,20,22)(H,21,25)(H,23,24)/p-1/t16-/m0/s1

Upstream product

• 70-47-3 L-asparagine 
• 88744-04-1 (9-fluorenyl)methyl pentafluorophenyl carbonate 
• 132388-59-1 L-Asn(Trt) 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 28920-44-7 (9H-fluoren-9-yl)methyl azidoformate 

Downstream Products

• 71989-17-8 N^α-fluorenylmethoxycarbonyl-L-asparagine p-nitrophenyl ester 
• 86060-99-3 N-α-Fmoc-L-asparagine pentafluorophenyl ester 
• 126402-76-4 [(S)-3-Carbamoyl-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionylamino]-acetic acid benzhydryl ester 
• 150047-86-2 (S)-2-[(S)-3-Carbamoyl-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionylamino]-4-methyl-pentanoic acid benzyl ester 
• 126771-42-4 (S)-2-(9H-Fluoren-9-ylmethoxycarbonylamino)-succinamic acid 4-(2,4-dichloro-phenoxycarbonylmethoxy)-benzyl ester 
• 181954-34-7 3-amino-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 200066-58-6 {5-[(S)-3-Carbamoyl-2-(9H-fluoren-9-ylmethoxycarbonylamino)-propionylamino]-pentyl}-carbamic acid tert-butyl ester 
• 313944-85-3 (S)-N^α-(Fluoren-9-ylmethoxycarbonyl)asparagine 4-methoxybenzyl ester 
• 857064-44-9 [2-carbamoyl-1-(2,3-dimethoxy-benzylcarbamoyl)-ethyl]-carbamic acid 9H-fluoren-9-ylmethyl ester 

Relevant articles and documents

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.

Optimized syntheses of Fmoc azido amino acids for the preparation of azidopeptides

The rise of CuI-catalyzed click chemistry has initiated an increased demand for azido and alkyne derivatives of amino acid as precursors for the synthesis of clicked peptides. However, the use of azido and alkyne amino acids in peptide chemistry is complicated by their high cost. For this reason, we investigated the possibility of the in-house preparation of a set of five Fmoc azido amino acids: β-azido l-alanine and d-alanine, γ-azido l-homoalanine, δ-azido l-ornithine and ω-azido l-lysine. We investigated several reaction pathways described in the literature, suggested several improvements and proposed several alternative routes for the synthesis of these compounds in high purity. Here, we demonstrate that multigram quantities of these Fmoc azido amino acids can be prepared within a week or two and at user-friendly costs. We also incorporated these azido amino acids into several model tripeptides, and we observed the formation of a new elimination product of the azido moiety upon conditions of prolonged couplings with 2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate/DIPEA. We hope that our detailed synthetic protocols will inspire some peptide chemists to prepare these Fmoc azido acids in their laboratories and will assist them in avoiding the too extensive costs of azidopeptide syntheses. Experimental procedures and/or analytical data for compounds 3–5, 20, 25, 26, 30 and 43–47 are provided in the supporting information.

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.

Basic techniques of working on a solid phase: From ABC of the peptide synthesis to libraries of non-natural amino acids

Libraries of hardly available amino acids bearing a heteroaromatic ring (2-pyrimidyl, substituted 2-pyridyl or 2-thiazolyl) at the amino group were prepared using solid-phase synthesis on various resins. The synthesized compounds are structurally similar to some known antidiabetic drugs. The paper combines features of a review (elementary introduction to the solid-phase synthesis methodology and technique for beginners and selected methods from peptide chemistry) and step-by-step experimental protocols (tested by the authors) useful as a methodic tool. The presented protocols (immobilization and modification of amino acids, placing and removal of common protective groups) require no sophisticated equipment and may be useful as pictorial introductory tasks for students education. Pleiades Publishing, Ltd., 2010.

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.

One-pot preparation of N-carbamate protected amino acids via the azide

A convenient and efficient method for the preparation of fluorenylmethyloxycarbonyl (Fmoc) and allyloxycarbonyl (Alloc) amino acids is proposed. This method is particularly attractive due to the fact that the reaction sequence Fmoc/Alloc-chloride to Fmoc/Alloc-azide to Fmoc/Alloc-amino acid can readily be carried out in one pot. A further advantage is the minimization of byproducts, which are easily removed during the workup. Most important, this strategy minimizes the formation of dipeptides that are difficult to remove by crystallization. Thus, Fmoc and Alloc amino acids are obtained in high yield (60-90%) and purity as evidenced by thin-layer chromatography, reversed-phase high-performance liquid chromatography, mass spectrometry, and nuclear magnetic resonance.

Apparatus and methods for detecting antibodies

A single, unitary, solid phase support apparatus having a planar surface divided into a plurality of separate zone functions to detect antibodies. Each zone has bonded to it, a different peptide through its C-terminal end. The zones are incubated with the analyte sample and observed for reaction, indicating the virus-specific or bacteria specific presence or absence.

Protection of carboxamide functions by the trityl residue. Application to peptide synthesis

Carboxamide functions may be tritylated by an acid-catalyzed reaction with triphenylmethanol and acetic anhydride in glacial acetic acid. The ω-trityl group of asparagine and glutamine is cleavable by TFA, but stable to strong mineral acids in aqueous solution, as well as to nucleophiles and bases. In peptide syntheses, it is ideally suited for combination with side-chain protections of the t.butyl-type.

9-Fluorenylmethyl Pentafluorophenyl Carbonate as a Useful Reagent for the Preparation of N-9-Fluorenylmethyloxycarbonylamino Acids and their Pentafluorophenyl Esters

9-Fluorenylmethyl pentafluorophenyl carbonate is a useful reagent for the efficient, side reaction-free introduction of N-9-fluorenylmethyloxycarbonyl protecting group into amino acids and for the subsequent preparation of their pentafluorophenyl esters.Some new compounds of both types are described.