1799443-50-7

Basic information

• Product Name: N-fluorenylmethoxycarbonyl-O-tertbutyl N-methyltyrosine
• CAS NO: 1799443-50-7
• Molecular Weight: 473.569
• Mol File: 1799443-50-7.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 638.9±55.0 °C(Predicted)
• Density: 1.208±0.06 g/cm3(Predicted)
• CAS DataBase Reference: N-fluorenylmethoxycarbonyl-O-tertbutyl N-methyltyrosine(CAS DataBase Reference)
• NIST Chemistry Reference: N-fluorenylmethoxycarbonyl-O-tertbutyl N-methyltyrosine(1799443-50-7)
• EPA Substance Registry System: N-fluorenylmethoxycarbonyl-O-tertbutyl N-methyltyrosine(1799443-50-7)

Safety Data

• Hazardous Substances Data: 1799443-50-7(Hazardous Substances Data)

Usage

Description

N-fluorenylmethoxycarbonyl-O-tertbutyl N-methyltyrosine is a synthetic compound used in peptide synthesis. It is a derivative of tyrosine, an amino acid that plays a crucial role in protein synthesis and various physiological processes. N-fluorenylmethoxycarbonyl-O-tertbutyl N-methyltyrosine has a tert-butyl and a fluorenylmethoxycarbonyl (Fmoc) protective group attached to the tyrosine residue, which allows for the selective and controlled addition of the amino acid to peptide chains. These protective groups can be removed under mild conditions, making N-fluorenylmethoxycarbonyl-O-tertbutyl N-methyltyrosine a versatile and useful building block for the synthesis of complex peptides in research and pharmaceutical applications.

Uses

Used in Pharmaceutical Industry:
N-fluorenylmethoxycarbonyl-O-tertbutyl N-methyltyrosine is used as a building block for the synthesis of complex peptides for various pharmaceutical applications. Its selective and controlled addition to peptide chains allows for the development of novel therapeutic agents with specific functions and properties.
Used in Research Applications:
N-fluorenylmethoxycarbonyl-O-tertbutyl N-methyltyrosine is used as a research tool for studying the structure and function of peptides and proteins. Its versatility and mild conditions for protective group removal make it a valuable compound for investigating the role of tyrosine-containing peptides in various biological processes.

Upstream product

• 1208119-58-7 N-methyl-N-nosyl-O-tert-butyl-L-tyrosine phenacyl ester 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 16879-90-6 N-[(benzyloxy)carbonyl]-O-(tert-butyl)-L-tyrosine, compound with dicyclohexylamine (1:1) 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 343631-38-9 C₁₄H₂₁NO₃ 
• 186581-53-3 diazomethane 
• 941296-83-9 N^α-nosyl-O-tert-butyl-L-tyrosine 
• 343631-38-9 (S)-3-(4-tert-Butoxy-phenyl)-2-methylamino-propionic acid 

Relevant articles and documents

Synthesis, experimental and in silico studies of N-fluorenylmethoxycarbonyl-O-tert-butyl-Nmethyltyrosine, coupled with CSD data: A survey of interactions in the crystal structures of Fmoc amino acids

Recently, fluorenylmethoxycarbonyl (Fmoc) amino acids (e.g. Fmoc tyrosine or Fmoc phenylalanine) have attracted growing interest in biomedical research and industry, with special emphasis directed towards the design and development of novel effective hydrogelators, biomaterials or therapeutics. With this in mind, a systematic knowledge of the structural and supramolecular features in recognition of those properties is essential. This work is the first comprehensive summary of noncovalent interactions combined with a library of supramolecular synthon patterns in all crystal structures of amino acids with the Fmoc moiety reported so far. Moreover, a new Fmoc-protected amino acid, namely, 2-{[(9H-fluoren-9-ylmethoxy)carbonyl](methyl)amino}-3-{4-[(2-hydroxypropan- 2-yl)oxy]phenyl}propanoic acid or N-fluorenylmethoxycarbonyl-O-tertbutyl-N-methyltyrosine, Fmoc-N-Me-Tyr(t-Bu)-OH, C29H31NO5, was successfully synthesized and the structure of its unsolvated form was determined by single-crystal X-ray diffraction. The structural, conformational and energy landscape was investigated in detail by combined experimental and in silico approaches, and further compared to N-Fmoc-phenylalanine [Draper et al. (2015). CrystEngComm, 42, 8047 8057]. Geometries were optimized by the density functional theory (DFT) method either in vacuo or in solutio. The polarizable conductor calculation model was exploited for the evaluation of the hydration effect. Hirshfeld surface analysis revealed that H H, C H/H C and O H/H O interactions constitute the major contributions to the total Hirshfeld surface area in all the investigated systems. The molecular electrostatic potentials mapped over the surfaces identified the electrostatic complementarities in the crystal packing. The prediction of weak hydrogenbonded patterns via Full Interaction Maps was computed. Supramolecular motifs formed via C H O, C H , (fluorenyl)C H Cl(I), C Br (fluorenyl) and C I (fluorenyl) interactions are observed. Basic synthons, in combination with the Long-Range Synthon Aufbau Modules, further supported by energy-framework calculations, are discussed. Furthermore, the relevance of Fmoc-based supramolecular hydrogen-bonding patterns in biocomplexes are emphasized, for the first time.

Solid-phase synthesis of N-nosyl- and N-Fmoc-N-methyl-α-amino acids

(Chemical Equation Presented) We report here a convenient and simple solid-phase synthesis of N-nosyl-N-methyl-α-amino acids and N-Fmoc-N-methyl-α-amino acids, important building blocks for the synthesis of conformationally restricted and protease-resista