24277-39-2

Basic information

• Product Name: Boc-L-glutamic acid 1-tert-butyl ester
• Synonyms: N-ALPHA-T-BUTOXYCARBONYL-L-GLUTAMIC ACID ALPHA-T-BUTYL ESTER;N-ALPHA-T-BOC-L-GLU-ALPHA-T-BUTYL ESTER;N-ALPHA-T-BOC-L-GLUTAMIC ACID ALPHA-T-BUTYL ESTER;N-ALPHA-TERT-BUTYLOXYCARBONYL-L-GLUTAMIC ACID-ALPHA-TERT-BUTYL ESTER;N-T-BUTOXYCARBONYL-L-GLUTAMIC ACID 1-T-BUTYL ESTER;N-T-BOC-L-GLUTAMIC ACID ALPHA-T-BUTYL ESTER;N-TERT-BUTOXYCARBONYL-L-GLUTAMIC ACID 1-TERT-BUTYL ESTER;N-T-boc-L-glutamic acid A-T-butyl-ester
• CAS NO: 24277-39-2
• Molecular Formula: C₁₄H₂₅NO₆
• Molecular Weight: 303.35
• Product Categories: Amino Acids;Glutamic acid [Glu, E];Boc-Amino Acids and Derivative
• Mol File: 24277-39-2.mol

Chemical Properties

• Melting Point: 111.0 to 115.0 °C
• Boiling Point: 449.8 °C at 760 mmHg
• Flash Point: 225.8 °C
• Appearance: white powder
• Density: 1.121 g/cm³
• Vapor Pressure: 2.42E-09mmHg at 25°C
• Refractive Index: 1.47
• Storage Temp.: −20°C
• Solubility: Soluble in dimethyl formamide.
• PKA: 4.48±0.10(Predicted)
• BRN: 3653769
• CAS DataBase Reference: Boc-L-glutamic acid 1-tert-butyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Boc-L-glutamic acid 1-tert-butyl ester(24277-39-2)
• EPA Substance Registry System: Boc-L-glutamic acid 1-tert-butyl ester(24277-39-2)

Safety Data

• Statements: 22/22-36/37/38
• Safety Statements: 4-7-28-35-44
• WGK Germany: 3
• Hazardous Substances Data: 24277-39-2(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Boc-L-glutamic acid 1-tert-butyl ester is used as a building block for the synthesis of various peptide-based drugs. Its incorporation into the peptide chain allows for the development of unique pharmaceutical compounds with specific biological activities, such as improved stability, enhanced bioavailability, or targeted drug delivery.
Used in Research and Development:
In the field of research and development, Boc-L-glutamic acid 1-tert-butyl ester serves as an essential component in the synthesis of novel peptides with potential applications in various therapeutic areas. Its use in solid-phase peptide synthesis (SPPS) enables the creation of peptides containing glutamate tert-butyl ester residues, which can be further modified or functionalized to explore new biological properties and potential therapeutic applications.
Used in Solid-Phase Peptide Synthesis (SPPS):
Boc-L-glutamic acid 1-tert-butyl ester is used as an N-terminal protected amino acid in solid-phase peptide synthesis (SPPS) to create unique peptides containing glutamate tert-butyl ester residues. This allows for the development of peptides with specific structural features and functional groups, which can be tailored to target specific biological processes or molecular interactions.

InChI:InChI=1/C14H25NO6/c1-13(2,3)20-11(18)9(7-8-10(16)17)15-12(19)21-14(4,5)6/h9H,7-8H2,1-6H3,(H,15,19)(H,16,17)/t9-/m0/s1

Upstream product

• 24277-38-1 (S)-(-)-1-tert-butyl-5-methyl-<(2-tert-butoxycarbonyl)amino>pentanedioate 
• 28812-54-6 N-tert-butoxyxarbonyl-L-glutamic acid γ-benzyl α-tert-butyl diester 
• 24424-99-5 di-tert-butyl dicarbonate 
• 611182-62-8 N-(diphenylmethylene)-L-glutamic acid 1-(1,1-dimethylethyl) 5-benzyl ester 
• 91229-91-3 tert-butyl (S)-N-tert-butoxycarbonylpyroglutamate 
• 56-86-0 L-glutamic acid 
• 1499-55-4 L-glutamic acid 5-methyl ester 
• 45214-91-3 (2S)-2-[(tert-butoxy)carbonylamino]-4-(methoxycarbonyl)butanoic acid 
• 81477-94-3 N-(diphenylmethylene)glycine tert-butyl ester 
• 1676-73-9 L-glutamic acid γ-benzyl ester 
• 80165-23-7 (S)-2-aminopentanedioic acid 5-benzyl ester 1-tert-butyl ester 
• 2791-84-6 L-glutamic acid dibenzyl ester 4-toluenesulfonate 
• 57732-63-5 1-tert-butyl 5-methyl (2S)-2-{[(benzyloxy)carbonyl]amino}pentanedioate 
• 79640-72-5 L-glutamic acid 1-tert-butyl ester 5-methyl ester 

Downstream Products

• 157886-31-2 (S,S)-2,7-bis<<(benzyloxy)carbonyl>amino>octanedioic acid 
• 73872-73-8 di-tert-butyl-di-Boc-diaminosuberate 
• 63061-86-9 α-tert-butyl N^α-Boc-N^α'-Cbz-α,α'-diaminosuberate 
• 91229-91-3 tert-butyl (S)-N-tert-butoxycarbonylpyroglutamate 
• 96304-42-6 trypanothione disulfide 
• 235438-56-9 N-(4-methoxyphenyl)methyl-N²-(t-butoxycarbonyl)-L-glutamine 1-t-butyl ester 
• 269733-29-1 (S)-6-tert-Butoxycarbonylamino-2-(triphenylphosphoranylidene)-3-oxoheptanedioic acid di-tert-butyl ester 
• 2387-23-7 1,3-Dicyclohexylurea 
• 189380-79-8 4-(2-hydroxyethylthioethyl)-L-glutamate 
• 284043-05-6 γ-O-(4-hydroxy-3-methoxyphenacetyl) t-butyl N-t-boc L-glutamate 
• 284043-08-9 γ-O-(3,5-dimethoxy-4-hydroxyphenacyl) t-butyl N-t-boc L-glutamate 
• 581800-01-3 2-tert-butoxycarbonylamino-4-{1-[2-tert-butoxycarbonyl-1-(1-tert-butoxycarbonyl-2-tritylsulfanyl-ethylcarbamoyl)-ethylcarbamoyl]-2-tritylsulfanyl-ethylcarbamoyl}-butyric acid tert-butyl ester 
• 91229-86-6 tert-butyl (S)-2-<(tert-butyloxycarbonyl)amino>-5-bromopentanoate 
• 674790-15-9 tert-butyl (S)-2-tert-butoxycarbonylamino-5-oxo-5-(4,4-dimethyl-2,6-dioxocyclohex-1-yl)pentanoate 

Relevant articles and documents

Synthesis of novel carboranyl derivatives of α-amino acids

New routes to closo-carboranyl derivatives of L-lysine and L-glutamic acid with free α-NH2 groups were proposed.

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

Synthesis and photochemical reactivity of caged glutamates with a π-extended coumarin chromophore as a photolabile protecting group

'Caging' and 'uncaging' bioactive substrates are key techniques in studying a wide variety of biological processes. In the present study, two-types of novel caged glutamates with a two-photon absorption (TPA) core, that is, π-extended coumarin, were synthesized and their photochemical release of glutamate was analyzed. The high yields of glutamate (>92%) were observed in the photolysis of compounds 1 and 10, respectively.

TRANSGLUTAMINASE 2 (TG2) INHIBITORS

Described herein are compounds and pharmaceutical compositions containing such compounds which inhibit transglutaminase 2 (TG2). Also described herein are methods for using such TG2 inhibitors, alone or in combination with other compounds, for treating diseases or conditions that would benefit from TG2 inhibition.

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(S)-Asparagine and (S)-glutamine ortho-carboranyl derivatives with free amino and carboxy groups in the α-position were synthesized. By an example of Nγ-(1,2-dicarba-closo-dodecarboran-3-yl)-(S)-glutamine it was demonstrated that the developed synthetic approach carboranyl derivatives of amino acids allowed the preparation of optically pure isomers.

LYSINE ISOTOPOLOGUES, COMPOSITIONS COMPRISING THE SAME AND METHODS OF SYNTHESIS

This invention relates to lysine isotopologues of Formulas I and 1-A, as described herein, and processes for synthesizing the same and derivatives and intermediates involved therein. In one aspect, described herein is a chemical compound comprising an isotopically labeled analog, i.e., an isotopologue of a standard or naturally occurring lysine. The lysine isotopologue is synthetically formed to have stable isotopes of elements incorporated at selected positions. As such, the lysine isotopologue has a molecular mass different from the mass of a standard or naturally occurring lysine.

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.

Caged glutamates with π-extended 1,2-dihydronaphthalene chromophore: Design, synthesis, two-photon absorption property, and photochemical reactivity

Caging and photochemical uncaging of the excitatory neurotransmitter l-glutamate (glu) offers a potentially valuable tool for understanding the mechanisms of neuronal processes. Designing water-soluble caged glutamates with the appropriate two-photon absorption property is an attractive strategy to achieve this. This paper describes the design, synthesis, and photochemical reactivity of caged glutamates with π-extended 1,2-dihydronaphthalene structures, which possess a two-photon cross-section of ～120 GM and an excellent buffer solubility (up to 115 mM). High yields up to 99% glutamate were observed in the photolysis of two caged glutamates. Suzuki-Miyaura cross-coupling and Buchwald-Hartwig amination were used as the key reactions to synthesize the caged compounds.

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Inhibition of glyoxalase I: The first low-nanomolar tight-binding inhibitors

A series of rational modifications to the structure of known S-(N-aryl-N-hydroxycarbamoyl)glutathione-based glyoxalase I inhibitors culminated in the discovery of the first single-digit nanomolar inhibitor. This study makes available key information about possible means to address the issues of metabolic instability, low potency, and synthetic complexicity that have plagued the area of glyoxalase I inhibition. Knowledge garnered from this study has implications in the design of inhibitors with higher conformational definition and lower peptidic character.