28812-54-6

Basic information

• Product Name: L-Glutamic acid, N-[(1,1-dimethylethoxy)carbonyl]-, 1-(1,1-dimethylethyl) 5-(phenylmethyl) ester
• CAS NO: 28812-54-6
• Molecular Formula: C21H31NO6
• Molecular Weight: 393.48
• Mol File: 28812-54-6.mol
• Article Data: 11

Chemical Properties

• CAS DataBase Reference: L-Glutamic acid, N-[(1,1-dimethylethoxy)carbonyl]-, 1-(1,1-dimethylethyl) 5-(phenylmethyl) ester(CAS DataBase Reference)
• NIST Chemistry Reference: L-Glutamic acid, N-[(1,1-dimethylethoxy)carbonyl]-, 1-(1,1-dimethylethyl) 5-(phenylmethyl) ester(28812-54-6)
• EPA Substance Registry System: L-Glutamic acid, N-[(1,1-dimethylethoxy)carbonyl]-, 1-(1,1-dimethylethyl) 5-(phenylmethyl) ester(28812-54-6)

Safety Data

• Hazardous Substances Data: 28812-54-6(Hazardous Substances Data)

Upstream product

• 24424-99-5 di-tert-butyl dicarbonate 
• 80165-23-7 (S)-2-aminopentanedioic acid 5-benzyl ester 1-tert-butyl ester 
• 80165-23-7 2-Amino-pentanedioic acid 5-benzyl ester 1-tert-butyl ester 
• 1676-73-9 glutamic acid γ-benzyl ester 
• 98946-18-0 tert-Butyl 2,2,2-trichloroacetimidate 
• 13574-13-5 Boc-Glu(OBzl)-OH 
• 24277-39-2 N-tert-butoxycarbonyl glutamic acid tert-butyl ester 
• 100-51-6 benzyl alcohol 
• 104-15-4 toluene-4-sulfonic acid 
• 2791-84-6 L-glutamic acid dibenzyl ester 4-toluenesulfonate 
• 1676-73-9 L-glutamic acid γ-benzyl ester 
• 56-86-0 L-glutamic acid 
• 91229-91-3 tert-butyl (S)-N-tert-butoxycarbonylpyroglutamate 
• 100-44-7 benzyl chloride 

Downstream Products

• 129241-86-7 (S)-2-glutarsaeure-5-benzyl-1-(tert-butyl)ester 
• 91229-90-2 α-tert-butyl N^α-(tert-butyloxycarbonyl)-N^δ-tosyl-N^δ-(benzyloxy)-L-ornithine 
• 37513-14-7 N^δ-tosyl-N^δ-(benzyloxy)-L-ornithine 
• 91229-91-3 α-tert-butyl N^α-(tert-butyloxycarbonyl)-L-pyroglutamate 
• 91229-86-6 tert-butyl (S)-2-<(tert-butyloxycarbonyl)amino>-5-bromopentanoate 
• 24277-39-2 α-tert-butyl N^α-(tert-butyloxycarbonyl)-L-glutamate 
• 197159-37-8 (S)-α-tert-butoxycarbonylamino-γ-(2,6-diphenylpyrimidin-4-yl)butyric acid α-tert-butyl ester 
• 197159-43-6 (S)-α-tert-butoxycarbonylamino-γ-(2-methylthio-6-phenylpyrimidin-4-yl)butyric acid α-tert-butyl ester 
• 197159-39-0 (S)-α-tert-butoxycarbonylamino-γ-(2-methyl-6-phenylpyrimidin-4-yl)butyric acid α-tert-butyl ester 
• 197159-27-6 (S)-2-tert-butoxycarbonylamino-5-oxo-7-phenylhept-6-ynoic acid tert-butyl ester 

Relevant articles and documents

Synthesis and biological evaluation of [18F](2S,4S)4-(3-fluoropropyl) arginine as a tumor imaging agent

Designing novel 18F-labeled amino acid derivatives for targeted amino acid transporters is an attractive strategy for the development of therapeutic and diagnostic agents for cancer therapy. In this work, we have developed a novel 3-fluoropropyl analog of arginine, namely, (2S,4S)4-[18F]FPArg, [18F]1, to be used as a probe for studying arginine metabolism. Optically pure and labeled with 18F and 19F, (2S,4S)4-(3-fluoropropyl)arginine was synthesized and isolated in high radiochemical purity (>95%). In vitro uptake assays in human MCF-7 cells revealed that [18F]1 enters cells mainly via sodium-independent cationic amino acid transporters and was inhibited >62% by arginine. [18F]1 showed a high cellular uptake of 7.3 ± 0.24% and 6.07 ± 0.3% uptake/100 mg protein after incubation in MCF-7 and MDA-MB-231 cells for 120 min, respectively. In vivo biodistribution studies demonstrated that [18F]1 provided high tumor uptake and high tumor to muscle ratios (5:1 at the 30 and 60 min time points). In vivo PET imaging studies demonstrated tumor-specific uptake in nude mice bearing MCF-7 breast tumors with an excellent tumor-to-muscle ratio. These results suggest that [18F]1 is a promising tracer for clinical breast cancer imaging and may be used to diagnose and monitor diseases that are associated with arginine metabolism.

Identification of SNAIL1 Peptide-Based Irreversible Lysine-Specific Demethylase 1-Selective Inactivators

Inhibition of lysine-specific demethylase 1 (LSD1), a flavin-dependent histone demethylase, has recently emerged as a new strategy for treating cancer and other diseases. LSD1 interacts physically with SNAIL1, a member of the SNAIL/SCRATCH family of transcription factors. This study describes the discovery of SNAIL1 peptide-based inactivators of LSD1. We designed and prepared SNAIL1 peptides bearing a propargyl amine, hydrazine, or phenylcyclopropane moiety. Among them, peptide 3, bearing hydrazine, displayed the most potent LSD1-inhibitory activity in enzyme assays. Kinetic study and mass spectrometric analysis indicated that peptide 3 is a mechanism-based LSD1 inhibitor. Furthermore, peptides 37 and 38, which consist of cell-membrane-permeable oligoarginine conjugated with peptide 3, induced a dose-dependent increase of dimethylated Lys4 of histone H3 in HeLa cells, suggesting that they are likely to exhibit LSD1-inhibitory activity intracellularly. In addition, peptide 37 decreased the viability of HeLa cells. We believe this new approach for targeting LSD1 provides a basis for development of potent selective inhibitors and biological probes for LSD1.

Analysis of density-dependent binding of glycans by lectins using carbohydrate microarrays

To investigate the density-dependent binding of glycans by lectins using carbohydrate microarrays, a number of C-terminal hydrazide-conjugated neoglycopeptides with various valences and different spatial arrangements of the sugar ligands were prepared on a solid support. The synthetic strategy includes (1) assembly of alkyne-linked peptides possessing C-terminal hydrazide on a solid support, (2) coupling of azide-linked, unprotected sugars to the alkyne-linked peptides on the solid support utilizing click chemistry, and (3) release of the neoglycopeptides from the solid support. By using this synthetic methodology, sixty five neoglycopeptides with a valency ranging from 1 to 4 and different spatial arrangements of the carbohydrate ligands were generated. Carbohydrate microarrays were constructed by immobilizing the prepared neoglycopeptides on epoxide-derivatized glass slides and were used to analyze the density-dependent binding of glycans by lectins. The results of binding property determinations show that lectin binding is highly dependent on the surface glycan density. Copyright