144701-24-6

Basic information

• Product Name: FMOC-D-NVA-OH
• Synonyms: Fmoc-D-NVal-OH;Fmoc-D-norvaline99%;N-ALPHA-(9-FLUORENYLMETHOXYCARBONYL)-D-NORVALINE;N-ALPHA-(9-FLUORENYLMETHOXYCARBONYL)-D-2-AMINOPENTANOIC ACID;N-ALPHA-FMOC-D-NORVALINE;RARECHEM EM WB 0171;FMOC-D-APE(2)-OH;FMOC-D-2-AMINOVALERIC ACID
• CAS NO: 144701-24-6
• Molecular Formula: C₂₀H₂₁NO₄
• Molecular Weight: 339.39
• Mol File: 144701-24-6.mol

Chemical Properties

• Melting Point: 152-154°C
• Boiling Point: 557.9 °C at 760 mmHg
• Flash Point: 291.2 °C
• Appearance: White powder
• Density: 1.23 g/cm³
• Storage Temp.: 2-8°C
• PKA: 3.91±0.20(Predicted)
• CAS DataBase Reference: FMOC-D-NVA-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-D-NVA-OH(144701-24-6)
• EPA Substance Registry System: FMOC-D-NVA-OH(144701-24-6)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• HazardClass: IRRITANT
• Hazardous Substances Data: 144701-24-6(Hazardous Substances Data)

Usage

Uses

Used in Organic Synthesis:
FMOC-D-NVA-OH is used as an intermediate for organic synthesis, particularly in the development of pharmaceuticals and other bioactive compounds. Its unique structure allows for the creation of complex molecules with specific properties, making it a valuable tool in the field of chemistry.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, FMOC-D-NVA-OH is used as a building block for the synthesis of various drugs and drug candidates. Its incorporation into the molecular structure can enhance the pharmacological properties of the final product, leading to improved efficacy and safety profiles.
Used in Peptide Synthesis:
FMOC-D-NVA-OH is also utilized in the synthesis of peptides, which are short chains of amino acids that serve as the building blocks of proteins. The D-configuration of the norvaline in FMOC-D-NVA-OH allows for the creation of non-natural peptides with unique properties, which can be used for various therapeutic applications.
Used in Research and Development:
In the field of research and development, FMOC-D-NVA-OH is employed as a reagent for the study of protein structure and function. Its ability to form stable peptide bonds and its compatibility with various chemical reactions make it an essential tool for understanding the complex interactions between proteins and other biomolecules.

Upstream product

• 2013-12-9 D-norvaline 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 1821-02-9 2-oxopentanoic acid 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 760-78-1 2-aminopentanoic acid 

Downstream Products

• 439082-60-7 (R)-2-propylpiperazine 
• 749250-57-5 C₃₀H₃₁N₃O₅ 

Relevant articles and documents

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.

Structure-guided engineering of: Meso -diaminopimelate dehydrogenase for enantioselective reductive amination of sterically bulky 2-keto acids

meso-Diaminopimelate dehydrogenase (DAPDH) and mutant enzymes are an excellent choice of biocatalysts for the conversion of 2-keto acids to the corresponding d-amino acids. However, their application in the enantioselective reductive amination of bulky 2-keto acids, such as phenylglyoxylic acid, 2-oxo-4-phenylbutyric acid, and indole-3-pyruvic acid, is still challenging. In this study, the structure-guided site-saturation mutagenesis of a Symbiobacterium thermophilum DAPDH (StDAPDH) gave rise to a double-site mutant W121L/H227I, which showed dramatically improved enzyme activities towards various 2-keto acids including these sterically bulky substrates. Several d-amino acids were prepared in optically pure form. The molecular docking of substrates into the active sites of wild-type and mutant W121L/H227I enzymes revealed that the substrate binding cavity of the mutant enzyme was reshaped to accommodate these bulky substrates, thus leading to higher enzyme activity. These results lay a foundation for further shaping the substrate binding pocket and manipulating the interactions between the substrate and binding sites to access highly active d-amino acid dehydrogenases for the preparation of synthetically challenging d-amino acids.

Sterically biased 3,3-sigmatropic rearrangement of azides: Efficient preparation of nonracemic α-amino acids and heterocycles

(Chemical Equation Presented) Homochiral α-amino acids, heterocycles, and carbocycles are efficiently constructed via a short sequence of reactions starting from the chiral auxiliary p-menthane-3-carboxaldehyde. The key feature of the sequence is a highly selective tandem Mitsunobu/3,3-sigmatropic rearrangement of hydrazoic acid that procures enantiomerically enriched allylic azides. The sequence is either terminated by oxidative cleavage to provide amino acids or by ring-closing metathesis to provide heterocycles or carbocycles bearing nitrogen.