3392-05-0

Basic information

• Product Name: Succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate
• Synonyms: BOC-D-ALA-OSU;BOC-D-ALANINE-OSU;BOC-D-ALANINE N-HYDROXYSUCCINIMIDE ESTER;BOC-D-ALANINE-HYDROXYSUCCINIMIDE ESTER;N-ALPHA-T-BOC-D-ALANINE N-HYDROXYSUCCINIMIDE ESTER;succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate;Boc-L-Alanine N-hydroxysuccinimde ester;BOC-L-ALA-OSU
• CAS NO: 3392-05-0
• Molecular Formula: C₁₂H₁₈N₂O₆
• Molecular Weight: 286.28
• EINECS: 222-229-7
• Product Categories: Amino Acid Derivatives;Amino Acids;Alanine [Ala, A];Boc-Amino Acids and Derivative;Boc-Amino acid series
• Mol File: 3392-05-0.mol

Chemical Properties

• Melting Point: 161-163 °C
• Appearance: /
• Density: 1.27 g/cm³
• Refractive Index: 1.51
• Storage Temp.: −20°C
• PKA: 10.81±0.46(Predicted)
• Sensitive: Moisture Sensitive
• BRN: 3560476
• CAS DataBase Reference: Succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate(CAS DataBase Reference)
• NIST Chemistry Reference: Succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate(3392-05-0)
• EPA Substance Registry System: Succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate(3392-05-0)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• F: 3-10-21
• Hazardous Substances Data: 3392-05-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate is used as a reactant for the synthesis of various pharmaceutical compounds, such as Muramyldipeptide analogs, Microcin C analogs, and N-Protected dipeptide acids. These analogs and derivatives have potential applications in the development of new drugs and therapies.
Used in Antibacterial Applications:
In the field of antibacterial research, Succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate is used as a reactant for the synthesis of Microcin C analogs. These analogs exhibit antibacterial properties, making them valuable in the development of new antibiotics to combat drug-resistant bacteria.
Used in Peptide Synthesis:
Succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate is used as a reactant in the synthesis of lipid I and nucleoside diphosphate peptide derivatives. These derivatives are essential in the study of peptide synthesis and have potential applications in the development of new peptide-based drugs.
Used in Cell Biology Research:
Succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate is used in the preparation of free and peptide-bound glycated amino acids. These glycated amino acids are crucial for studying their interactions with human Caco-2 intestinal epithelial cell apical membrane transport proteins, which can provide insights into the mechanisms of cellular transport and the development of new therapeutic strategies.
Used in Cancer Research:
In the field of cancer research, Succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate is used as a reactant for the synthesis of 7-Substituted camptothecin conjugates with RGD-peptides. These conjugates serve as avβ3 integrin ligands, which can be used to target specific cancer cells, potentially improving the efficacy of cancer treatments.
Used in Organic Chemistry:
Succinimido (S)-2-[(tert-butoxycarbonyl)amino]propionate is used as a versatile building block in organic chemistry, allowing researchers to synthesize a wide range of compounds with various applications in different industries, including pharmaceuticals, materials science, and biotechnology.

InChI:InChI=1/C12H18N2O6/c1-7(13-11(18)19-12(2,3)4)10(17)20-14-8(15)5-6-9(14)16/h7H,5-6H2,1-4H3,(H,13,18)

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 15761-38-3 L-N-Boc-Ala 
• 75513-55-2 N-hydroxysuccinimido diphenyl phosphate 
• 107960-02-1 1,2,2,2-tetrachloroethyl-(N-succinimidyl)carbonate 
• 90704-86-2 bis(N-hydroxysuccinimide) sulfite 
• 16948-17-7 Boc-Ala-OH*DCHA 
• 3744-87-4 Boc-(R)-Ala 
• 58632-95-4 2-(tert-Butoxycarbonyloxyimino)-2-phenylacetonitrile 
• 77422-40-3 tert-butyloxycarbonylalanyl-4-pyridylmethylester 
• 24424-99-5 di-tert-butyl dicarbonate 

Downstream Products

• 23632-78-2 N-tert-butyloxycarbonyl-L-alanyl-glycine benzyl ester 
• 57177-77-2 Boc-Ala-Lys(Boc)-NHNH-Z 
• 2448-58-0 (S)-2-((S)-2-((tert-butoxycarbonyl)amino)propanamido)-3-phenylpropanoic acid 
• 98919-97-2 (2S,6S)-2-Amino-6-((S)-2-tert-butoxycarbonylamino-propionylamino)-heptanedioic acid 
• 142811-55-0 ((S)-1-{3,5-Bis-[((S)-2-tert-butoxycarbonylamino-propionylamino)-methyl]-benzylcarbamoyl}-ethyl)-carbamic acid tert-butyl ester 
• 114856-02-9 Boc-Ala-Lys(Z)-OBzl 
• 56618-30-5 N-(tert-butoxycarbonyl)-L-alanyl-L-leucine benzyl ester 
• 19794-10-6 (S)-methyl 2-((S)-2-((tert-butoxycarbonyl)amino)propanamido)propanoate 
• 129121-69-3 [(S)-1-(4-{Benzyloxycarbonyl-[2-(5-{2-[2-(2,4-bis-benzyloxy-phenyl)-acetylamino]-3-carbamoyl-propionylamino}-pentylcarbamoyl)-ethyl]-amino}-butylcarbamoyl)-ethyl]-carbamic acid tert-butyl ester 
• 73870-83-4 Boc-Ala-Gly-Gly-OBzl 
• 59524-71-9 t-butoxycarbonyl-L-alanyl-L-glutamic acid dibenzyl ester 
• 18814-49-8 tert-butoxycarbonyl-L-alanyl-D-isoglutamine benzyl ester 
• 18671-06-2 N-t-butoxycarbonyl-L-alanyl-L-alanyl-L-alanine benzyl ester 
• 114117-77-0 Boc-Ala-Lys(Z)-Lys(Z)-OPac 

Relevant articles and documents

Synthesis of conjugates of glyco amino acids and glycopeptides with carboxylic acid hydrazides

It is proposed to use a hydrazine "bridge" for obtaining conjugates of glycopeptides with biologically active carboxylic acids. Diacylhydrazines have been synthesized from glucofuranosylglycoloyl-L-alanine and β-butylmuramoyltripeptide.

Synthesis of pyrimidine nucleoside and amino acid conjugates

The synthesis of novel pyrimidine nucleoside bioconjugates with amino acids is presented. The N4-amino acid-acylated 2′-deoxycytidine analogues, modified with various amino acids, were synthesized using a three-step synthesis and obtained in moderate overall yields. Novel amino acid-alkylated 2′-deoxycytidine derivatives were obtained during the rearrangement of amino acid-acylated derivatives that occurred during Boc deprotection.

Ynamide-Mediated Thiopeptide Synthesis

Exploration of the full potential of thioamide substitution as a tool in the chemical biology of peptides and proteins has been hampered by insufficient synthetic strategies for the site-specific introduction of a thioamide bond into a peptide backbone. A novel ynamide-mediated two-step strategy for thiopeptide bond formation with readily available monothiocarboxylic acids as thioacyl donors is described. The α-thioacyloxyenamide intermediates formed from the ynamides and monothiocarboxylic acids can be purified, characterized, and stored. The balance between their activity and stability enables them to act as effective thioacylating reagents to afford thiopeptide bonds under mild reaction conditions. Amino acid functional groups such as OH, CONH2, and indole NH groups need not be protected during thiopeptide synthesis. The modular nature of this strategy enables the site-specific incorporation of a thioamide bond into peptide backbones in both solution and the solid phase.

Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome

Antibiotic chloramphenicol (CHL) binds with a moderate affinity at the peptidyl transferase center of the bacterial ribosome and inhibits peptide bond formation. As an approach for modifying and potentially improving properties of this inhibitor, we explored ribosome binding and inhibitory activity of a number of amino acid analogs of CHL. The L-histidyl analog binds to the ribosome with the affinity exceeding that of CHL by 10 fold. Several of the newly synthesized analogs were able to inhibit protein synthesis and exhibited the mode of action that was distinct from the action of CHL. However, the inhibitory properties of the semi-synthetic CHL analogs did not correlate with their affinity and in general, the amino acid analogs of CHL were less active inhibitors of translation in comparison with the original antibiotic. The X-ray crystal structures of the Thermus thermophilus 70S ribosome in complex with three semi-synthetic analogs showed that CHL derivatives bind at the peptidyl transferase center, where the aminoacyl moiety of the tested compounds established idiosyncratic interactions with rRNA. Although still fairly inefficient inhibitors of translation, the synthesized compounds represent promising chemical scaffolds that target the peptidyl transferase center of the ribosome and potentially are suitable for further exploration.

CHEMICAL SYNTHESIS AND ANTI-TUMOR AND ANTI-METASTATIC EFFECTS OF DUAL FUNCTIONAL CONJUGATE

The present invention discloses chemical synthesis, anti-tumor and anti-metastatic effects of a dual functional conjugate as showed by formula I. In detail, paclitaxel or docetaxol is linked with muramyl dipeptide derivative to form a conjugate, thus dual anti-tumor and anti-metastatic effects are achieved by combination of chemotherapy and immunotherapy. The present invention also discloses that paclitaxel or docetaxol and muramyl dipeptide derivative conjugate is synthesized by combination of solid-phase and solution-phase synthesis, and said conjugate can be used in manufacture of anti-tumor medicaments as proved by reliable bioassays.

N,O-Bis(trimethylsilyl)acetamide/N-hydroxysuccinimide ester (BSA/NHS) as coupling agents for dipeptide synthesis

A method using N,O-bis(trimethylsilyl)acetamide/N-hydroxysuccinimide ester (BSA/NHS) as coupling agents for dipeptide synthesis is descried. The coupling reaction between N-hydroxysuccinimide (NHS) esters and amines could be performed under mild conditions with N,O-bis(trimethylsilyl)acetamide (BSA) as coupling reagent and no additional acid/base is required. All byproducts and excessive reactants are water soluble or hydrolysable and easy to eliminate through water-washing at the purification stage. Moreover, all the reactants are inexpensive and widely used in conventional drug production.

Synthetic tripeptides as alternate substrates of murein peptide ligase (Mpl)

Murein peptide ligase (Mpl) is an enzyme found in Gram-negative bacteria. It catalyses the addition of tripeptide l-Ala-γ-d-Glu-meso-diaminopimelate to nucleotide precursor UDP-N-acetylmuramic acid during the recycling of peptidoglycan. Although not essential, this enzyme represents an interesting target for antibacterial compounds through the synthesis of alternate substrates whose incorporation into peptidoglycan might be deleterious for the bacterial cell. Therefore, we have synthesised 10 tripeptides l-Ala-γ-d-Glu-Xaa in which Xaa represents amino acids different from diaminopimelic acid. Tripeptide with Xaa = ε-d-Lys proved to be an excellent substrate of Escherichia coli Mpl in vitro. Tripeptides with Xaa = p-amino- or p-nitro-l-phenylalanine were poor substrates, while tripeptides with Xaa = d- or l-2-aminopimelate, dl-2-aminoheptanoic acid, l-Glu, l-norleucine, l-norvaline, l-2-aminobutyric acid or l-Ala were not substrates at all. Although a good Mpl substrate, the d-Lys-containing tripeptide was devoid of antibacterial activity against E. coli, presumably owing to poor uptake.

A mild method for the cleavage of the 4-picolyloxy group with magnesium under neutral conditions

A mild and efficient method for the selective hydrolysis of 4-picolyl esters with magnesium in methanol or water in the presence of other esters and sensitive protecting groups is described. 4-Picolyl aryl ethers and thioethers are also smoothly deprotected to give the corresponding phenols and thiophenols. Georg Thieme Verlag Stuttgart. New York.

A facile synthesis and crystallographic analysis of N-protected β-amino alcohols and short peptaibols

A facile, efficient and racemization-free method for the synthesis of N-protected β-amino alcohols and peptaibols using N-hydroxysuccinimide active esters is described. Using this method, dipeptide, tripeptide and pentapeptide alcohols were isolated in high yields. The conformations in crystals of β-amino alcohol, dipeptide and tripeptide alcohols were analysed, with a well-defined type III β-turn being observed in the tripeptide alcohol crystals. This method is found to be compatible with Fmoc-, Boc- and other side-chain protecting groups.

Solution-phase synthesis of a muramyl dipeptide analogue MDA

The solution-phase synthesis of a muramyl dipeptide (MDP) analogue of Nα-[4-chlorocinnamoyl-l-alanyl-d-isoglutaminyl]-l-lysine (MDA, 2) is reported that possesses the features of easy feasibility, safety and low cost in large scale of synthesis.