119062-05-4

Basic information

• Product Name: Fmoc-L-aspartic acid
• Synonyms: (S)-2-((((9H-fluoren-9-yl)Methoxy)carbonyl)aMino)succinic acid;N-FMoc-L-AspaD23-Ragine;Fmoc-L-aspartic acid≥ 99% (HPLC);N-(9-FLUORENYLMETHOXYCARBONYL)-L-ASPARTIC ACID;N-[(9H-FLUOREN-9-YLMETHOXY)CARBONYL]-L-ASPARTIC ACID;N-ALPHA-(9-FLUORENYLMETHOXYCARBONYL)-L-ASPARTIC ACID;N-FMOC-L-ASPARTIC ACID;FMOC-L-ASP-OH
• CAS NO: 119062-05-4
• Molecular Formula: C₁₉H₁₇NO₆
• Molecular Weight: 355.34
• EINECS: 1533716-785-6
• Product Categories: Isoquinolines ,Quinolines ,Quinaldines;Amino Acid Derivatives;Amino Acids;Aspartic acid [Asp, D];Fmoc-Amino Acids and Derivatives;Amino Acids (N-Protected);Biochemistry;Fmoc-Amino Acids;Fmoc-Amino acid series;A - H;Amino Acids;Modified Amino Acids
• Mol File: 119062-05-4.mol

Chemical Properties

• Melting Point: 180-190 °C
• Boiling Point: 587.2 °C at 760 mmHg
• Flash Point: 308.9 °C
• Appearance: /
• Density: 1.399 g/cm³
• Vapor Pressure: 1.24E-14mmHg at 25°C
• Refractive Index: 1.628
• Storage Temp.: −20°C
• PKA: 3.66±0.23(Predicted)
• Water Solubility: Soluble in methanol, and water.
• CAS DataBase Reference: Fmoc-L-aspartic acid(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-L-aspartic acid(119062-05-4)
• EPA Substance Registry System: Fmoc-L-aspartic acid(119062-05-4)

Safety Data

• Safety Statements: 24/25
• WGK Germany: 3
• Hazardous Substances Data: 119062-05-4(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Fmoc-L-aspartic acid is used as a building block for the synthesis of peptides and proteins. Its Fmoc protecting group allows for the stepwise assembly of peptide chains, facilitating the controlled and efficient synthesis of complex biological molecules. This is particularly important in the development of new drugs and therapeutic agents.
Used in Biochemical Research:
In biochemical research, Fmoc-L-aspartic acid serves as a reagent for the study of protein structure and function. Its ability to be incorporated into peptides and proteins allows researchers to investigate the role of specific amino acid sequences in biological processes and to develop a deeper understanding of molecular interactions.
Used in Food Industry:
Fmoc-L-aspartic acid is used as a flavor enhancer in the food industry. It can be used to improve the taste of various food products by mimicking the natural umami taste, which is associated with the savory flavor found in certain foods such as meat, cheese, and tomatoes.
Used in Cosmetics Industry:
In the cosmetics industry, Fmoc-L-aspartic acid is used as an ingredient in skincare products. Its ability to bind with other molecules can help improve the texture and feel of cosmetic formulations, providing a smoother and more pleasant application experience for consumers.
Used in Biomaterials and Tissue Engineering:
Fmoc-L-aspartic acid is used in the development of biomaterials and tissue engineering applications. Its ability to form stable complexes with other molecules can be leveraged to create materials with specific properties, such as controlled degradation rates or enhanced biocompatibility, which are essential for medical implants and tissue scaffolds.

InChI:InChI=1/C19H17NO6/c21-17(22)9-16(18(23)24)20-19(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,(H,20,25)(H,21,22)(H,23,24)/t16-/m0/s1

Upstream product

• 56-84-8 L-Aspartic acid 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 129460-09-9 Fmoc-Asp-O-t-Bu 
• 102774-86-7 9-fluorenylmethyl N-succinimidyl carbonate 
• 71989-14-5 Fmoc-(tBu)Asp-OH 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 1415814-25-3 (7-N,N-diethylaminocoumarin-4-yl)-methyl-N-(9-fluorenylmethyloxycarbonyl)aspartic acid 
• 1415814-26-4 Fmoc-Asp(DEACE)-OH 
• 146982-24-3 N-alpha-(9-fluorenylmethyloxycarbonyl)-L-aspartic acid beta-allyl ester 

Downstream Products

• 119062-06-5 (S)-3-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-4-(((S)-3-(4-hydroxyphenyl)-1-methoxy-1-oxopropan-2-yl)amino)-4-oxobutanoic acid 

Relevant articles and documents

Profiling primary protease specificity by peptide synthesis on a solid support

Reverse screening: A greatly simplified primary screening of protease specificity has been achieved by monitoring the fluorescence during the protease-catalyzed coupling of amino acids instead of peptide hydrolysis on a solid support (see picture, AA = amino acid). This approach paves the way for flexible, rapid, high-throughput identification and characterization of proteases without the need for expensively labeled peptide arrays.

Reaction of N-Fmoc aspartic anhydride with glycosylamines: a simple entry to N-glycosyl asparagines

The reaction of N-Fmoc-aspartic anhydride with glycosyl amines in DMSO selectively leads to the formation of β-substituted products, thus providing a simple and efficient route to N-glycosyl asparagine derivatives, the building blocks for glycopeptide synthesis.

A new polymer-supported reagent for the Fmoc-protection of amino acids

A new polymer-supported Fmoc-OSu (Fmoc-P-OSu) has been prepared from polymer-bound N-hydroxysuccinimide (P-HOSu), and used as a solid-supported reagent for the Fmoc-protection of amino groups. The residual P-HOSu generated after the protection reaction can be separated by simple filtration and reused.

MgI2-Mediated Chemoselective Cleavage of Protecting Groups: An Alternative to Conventional Deprotection Methodologies

The scope of MgI2 as a valuable tool for quantitative and mild chemoselective cleavage of protecting groups is described here. This novel synthetic approach expands the use of protecting groups, widens the concept of orthogonality in synthetic processes, and offers a facile opportunity to release compounds from solid supports. Amazing MgI2: Protecting groups have had a tremendous positive impact on the art of biomolecule synthesis. In a context in which the use of attractive protecting groups is often limited by harsh deprotection conditions and low chemoselective flexibility, MgI2 offers, by the execution of a very simple protocol, a fresh vision with extensive perspectives.

Ethyl substituted coumarin-4-yl derivatives as photoremovable protecting groups for amino acids with improved stability for SPPS

The synthesis, photochemical properties and chemical stability of 7-(N,N-diethylamino-coumarin-4-yl)-1-ethyl (DEACE) photoremovable protecting group for carboxylic acids are presented. We demonstrate that the ethyl substituent of DEACE improves the hydrolytic stability of the protected ester in basic conditions used in solid phase peptide synthesis (SPPS) and retains the good photochemical properties of the coumarin-4-yl methyl derivatives. DEACE allows the preparation of peptides with protected carboxylic side groups with high yield via 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.

A microwave-assisted synthesis of (S)-N-protected homoserine γ-lactones from l-aspartic acid

A three-pot preparation of (S)-N-protected homoserine γ-lactones is presented. Conversion of N-protected l-aspartic acid to an oxazolidinone is followed by selective reduction/acid-catalyzed cyclization to deliver the lactones. Microwave irradiation proved valuable for improving the latter reaction steps in some cases.

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.

Identification of small peptides mimicking the R2 C-terminus of Mycobacterium tuberculosis ribonucleotide reductase

Ribonucleotide reductase (RNR) is a viable target for new drugs against the causative agent of tuberculosis, Mycobacterium tuberculosis. Previous work has shown that an N-acetylated heptapeptide based on the C-terminal sequence of the smaller RNR subunit can disrupt the formation of the holoenzyme sufficiently to inhibit its function. Here the synthesis and binding affinity, evaluated by competitive fluorescence polarization, of several truncated and N-protected peptides are described. The protected single-amino acid Fmoc-Trp shows binding affinity comparable to the N-acetylated heptapeptide, making it an attractive candidate for further development of non-peptidic RNR inhibitors. Copyright

Amphiphilic cyclodextrin derivatives, method for preparation thereof and uses thereof

The invention relates to cyclodextrin derivatives of formula (I): in which: R1═—NH-E-AA-(L1)p(L2)q where E=a linear or branched Cl-Cl5 hydrocarbon-based group with, optionally, one or more hetero atoms; AA=the residue of an amino acid; L1 and L2=a C6-C24 hydrocarbon-based group with, optionally, one or more hetero atoms; p and q=0 or 1, at least one being ≠0; R2═H, —CH3, isopropyl, hydroxypropyl, sulphobutyl ether; R3═H or R2, except when R2=hydroxypropyl; all the R4═—OH or R2, except when R2=hydroxypropyl, or at least one of the R4═R1; n=5, 6 or 7. The invention also relates to a process for preparing them, and to inclusion complexes and organized surfactant systems comprising them.