200623-62-7

Basic information

• Product Name: N-Fmoc-N'-trityl-D-glutamine
• Synonyms: FMOC-D-GLN(TRT)-OH;FMOC-D-GLN(TRT);FMOC-D-GLUTAMINE(TRITYL);FMOC-D-GLUTAMINE(TRT)-OH;FMOC-N-DELTA-TRITYL-D-GLUTAMINE;N-ALPHA-FMOC-N-GAMMA-TRITYL-D-GLUTAMINE;N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-N-GAMMA-TRITYL-D-GLUTAMINE;N-ALPHA-9-FLUORENYLMETHOXYCARBONYL-N-OMEGA-TRITYL-D-GLUTAMINE
• CAS NO: 200623-62-7
• Molecular Formula: C39H34N2O5
• Molecular Weight: 610.7
• Product Categories: Amino Acids;Glutamine [Gln, Q];Fmoc-Amino Acids and Derivatives;Fmoc-Amino acid series
• Mol File: 200623-62-7.mol

Chemical Properties

• Melting Point: 232-237°C
• Boiling Point: 873.5 °C at 760 mmHg
• Flash Point: 482.1 °C
• Appearance: /
• Density: 1.256
• Storage Temp.: -20°C
• Solubility: Acetonitrile (Slightly), Chloroform (Slightly), DMF (Sparingly)
• PKA: 3.73±0.10(Predicted)
• CAS DataBase Reference: N-Fmoc-N'-trityl-D-glutamine(CAS DataBase Reference)
• NIST Chemistry Reference: N-Fmoc-N'-trityl-D-glutamine(200623-62-7)
• EPA Substance Registry System: N-Fmoc-N'-trityl-D-glutamine(200623-62-7)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 200623-62-7(Hazardous Substances Data)

Usage

Uses

Used in Chemical Synthesis:
N-Fmoc-N'-trityl-D-glutamine is used as a building block for the synthesis of various complex molecules, including pharmaceuticals and bioactive compounds. Its application in this field is attributed to its compatibility with a wide range of chemical reactions and its ability to be easily incorporated into larger molecular structures.
Used in Peptide Chemistry:
In peptide chemistry, N-Fmoc-N'-trityl-D-glutamine serves as a crucial component in the construction of peptide sequences. It is used as a protected amino acid, which aids in the stepwise assembly of peptides while preventing unwanted side reactions. The trityl group provides a stable protection for the amino group, ensuring the selective deprotection and coupling of subsequent amino acids during peptide synthesis.
Used in Pharmaceutical Industry:
N-Fmoc-N'-trityl-D-glutamine is used as a key intermediate in the development of novel drugs and therapeutic agents. Its application in this industry is due to its ability to be modified and incorporated into various drug candidates, potentially leading to the discovery of new treatments for a range of diseases and conditions.
Used in Research and Development:
In the field of research and development, N-Fmoc-N'-trityl-D-glutamine is utilized as a valuable tool for studying the properties and functions of amino acids and peptides. Its use in this context allows scientists to gain a deeper understanding of the molecular mechanisms underlying various biological processes and to develop new strategies for targeting specific biological pathways.

Upstream product

• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 102747-84-2 5-trityl-L-glutamine 
• 76-84-6 triphenylmethyl alcohol 
• 56-85-9 L-glutamine 
• 2650-64-8 Cbz-L-Gln 
• 132388-60-4 (S)-2-(((benzyloxy)carbonyl)amino)-5-oxo-5-(tritylamino)pentanoic acid 
• 71989-20-3 N₂-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-glutamine 

Downstream Products

• 132388-65-9 Fmoc-Gln(Trt)-OPfp 
• 494771-03-8 1-[19-amino-5-sec-butyl-8-(2-carbamoyl-ethyl)-11-carbamoylmethyl-2-(4-hydroxy-benzyl)-3,6,9,12,20-pentaoxo-1,4,7,10,13pentaaza-cycloeicos-16-ene-14-carbonyl]-pyrrolidine-2-carboxylic acid [1-(carbamoylmethyl-carbamoyl)-3-methyl-butyl]-amide 

Relevant articles and documents

Caged xanthones: Potent inhibitors of global predominant MRSA USA300

Total of 22 caged xanthones were subjected to susceptibility testing of global epidemic MRSA USA300. Natural morellic acid showed the strongest potency (MIC of 12.5 μM). However, its potent toxicity diminishes MRSA therapeutic potential. We synthetically modified natural morellic acid to yield 13 derivatives (3a-3m). Synthetically modified 3b retained strong potency in MRSA growth inhibition, yet the toxicity was 20-fold less than natural morellic acid, permitting the possibility of using caged xanthones for MRSA therapeutic.

Mild oxidative cleavage of 9-BBN-protected amino acid derivatives

Protection of the amino acid moiety using 9-BBN is an effective method to enable side chain manipulations in synthesis of complex amino acids. We investigated the standard, mild method for deprotection of the 9-BBN group in methanolic chloroform, and found that it relies on a slow oxidation mediated by molecular oxygen. Building on this insight, we have developed a method that allows for a fast and selective deprotection using simple peroxy acid reagents. After Fmoc protection, products were isolated in >90% yield for a series of amino acid derivatives, including a galactosylated derivative of hydroxylysine. A representative set of 9-BBN-protected amino acid derivatives were efficiently deprotected using peracid reagents in excellent yields. Deprotection is orthogonal with several common protecting groups. Its tolerance of highly acid sensitive groups, such as trityl-protected amides and glycosidic linkages, is especially notable.

NOVEL PEPTIDES DERIVED FROM NCAM (FGLs)

The present invention relates to novel compounds comprising at most 13 contiguous amino acid residues derived from the fibronectin type 3,I1 module of neural cell adhesion molecule (NCAM), or a variant or fragment thereof, capable of interacting with an FGFR and thereby the compounds are capable of inducing differentiation, modulating proliferation, stimulate regeneration, neuronal plasticity and/or survival of cells. Further, the present invention relates to the use of said compounds for production of a medicament for treatment of conditions and diseases, wherein NCAM and/or FGFR play a prominent role.

DIPHENYLMETHANE COMPOUND

Compounds having a diphenylmethane skeleton are superior in broad utility and stability, and are useful as a protecting reagent (anchor) of amino acid and/or peptide in the liquid phase synthesis and the like of a peptide having a C-terminal etc., which are of a carboxamide(-CONHR)-type, and in organic synthetic reaction methods (particularly peptide liquid phase synthetic methods), and may be contained in a kit for peptide liquid phase synthesis.

GLP-2 compounds, formulations, and uses thereof

The present invention relates to novel human glucagon-like peptide-2 (GLP-2) peptides and human glucagon-like peptide-2 derivatives which have a protracted profile of action as well as polynucleotide constructs encoding such peptides, vectors and host cells comprising and expressing the polynucleotide, pharmaceutical compositions, uses and methods of treatment.

Antiangiogenic peptides

Mammalian kringle 5 fragments and kringle 5 fusion proteins are disclosed as a compounds for treating angiogenic diseases. Methods and compositions for inhibiting angiogenic diseases are also disclosed.

Flanking peptides of calcitonin and processes for their manufacture

Peptides of formula I STR1 in which R is hydrogen or acetyl and X is an amino acid sequence of formula -Ser-Leu-Asp-Ser-Pro-Arg-Ser- (Ia) or of formula -Arg-Ile-Ile-Ala-Gln- (Ib), and salts of such compounds, can be used for the treatment of diseases involving bone degeneration.

Protected amino acids and process for the preparation thereof

Compounds of the formula I, STR1 in which 'R1 is an amino protective group, and n stands for 1 or 2, R1 denotes hydrogen or an amino protective group, R2 denotes hydrogen or a carboxyl protective group and R3 denotes triphenylmethyl, 4-monomethoxy-trityl or 4,4'-dimethoxy-trityl, and reactive carboxylic acid derivatives of such compounds of the formula I in which R2 stands for hydrogen, are described. These compounds can be used as starting materials for the preparation of peptides. They are more suitable for this than are analogous compounds of the formula I in which R3 denotes hydrogen or one of the carbamoyl protective groups hitherto customary.

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.