141-36-6

Usage

Uses

Used in Pharmaceutical Synthesis:
(+/-)-TRANS-EPOXYSUCCINIC ACID is used as a key intermediate in the synthesis of pharmaceuticals for its ability to undergo various chemical transformations, contributing to the development of new drugs with potential therapeutic benefits.
Used in Agrochemical Production:
In the agrochemical industry, (+/-)-TRANS-EPOXYSUCCINIC ACID is utilized as a starting material or intermediate in the production of various agrochemicals, aiding in the creation of compounds that can enhance crop protection and yield.
Used in Organic Chemical Reactions:
(+/-)-TRANS-EPOXYSUCCINIC ACID serves as a reactant in organic chemical reactions, where its unique epoxide group allows for the formation of new compounds with potential applications in various fields.
Used in Drug Discovery and Development:
(+/-)-TRANS-EPOXYSUCCINIC ACID and its derivatives are used as potential candidates in drug discovery and development due to their studied anti-inflammatory and anti-cancer properties, offering new avenues for therapeutic intervention in medical treatments.

InChI:InChI=1/C4H4O5/c5-3(6)1-2(9-1)4(7)8/h1-2H,(H,5,6)(H,7,8)/t1-,2-/m0/s1

Upstream product

• 110-17-8 (2E)-but-2-enedioic acid 
• 17087-75-1 (-)-trans-2,3-oxiranedicarboxylic acid 
• 17015-08-6 (2R,3R)-oxirane-2,3-dicarboxylic acid 
• 75-91-2 tert.-butylhydroperoxide 
• 624-49-7 dimethylfumarate 
• 3291-46-1 (2SR,3SR)-oxirane-2,3-dicarboxylic acid diethyl ester 

Downstream Products

• 17087-75-1 (-)-trans-2,3-oxiranedicarboxylic acid 
• 17015-08-6 (2R,3R)-oxirane-2,3-dicarboxylic acid 
• 6463-75-8 N-(DL-α-Methyl-benzyl)-erythro-β-hydroxy-DL-asparaginsaeure 
• 1186-90-9 erythro-β-hydroxy-DL-aspartic acid 
• 133-37-9 DL-tartaric acid 
• 87-69-4 tartaric acid 
• 75-07-0 acetaldehyde 
• 3291-46-1 (2SR,3SR)-oxirane-2,3-dicarboxylic acid diethyl ester 
• 3291-46-1 (2S,3S)-diethyl oxirane-2,3-dicarboxylate 
• 16417-32-6 N-benzyl-erythro-β-hydroxy-DL-aspartic acid 

Relevant academic research and scientific papers

Design, Synthesis, and Evaluation of Aza-Peptide Epoxides as Selective and Potent Inhibitors of Caspases-1, -3, -6, and -8

Aza-peptide epoxides, a novel class of irreversible protease inhibitors, are specific for the clan CD cysteine proteases. Aza-peptide epoxides with an aza-Asp residue at P1 are excellent irreversible inhibitors of caspases-1, -3, -6, and -8 with second-order inhibition rates up to 1 910 000 M-1 s-1. In general, the order of reactivity of aza-peptide epoxides is S,S > R,R > trans > cis. Interestingly, some of the R,R epoxides while being less potent are actually more selective than the S,S epoxides. Our aza-peptide epoxides designed for caspases are stable, potent, and specific inhibitors, as they show little to no inhibition of other proteases such as the aspartyl proteases porcine pepsin, human cathepsin D, plasmepsin 2 from P. falciparum, HIV-1 protease, and the secreted aspartic proteinase 2 (SAP-2) from Candida albicans; the serine proteases granzyme B and α-chymotrypsin; and the cysteine proteases cathepsin B and papain (clan CA), and legumain (clan CD).

Configuration and enantioselective synthesis of the fungal metabolite WF14861

A short enantioselective synthesis of the cathepsine inhibitor WF14861 (1) from the funghi Colletotrichum sp. as well as of its diasteroisomer 21 is presented. Comparison of the NMR data of the final products and, in particular, of the [α]D values of the intermediates allowed the confirmation of the formerly proposed structure 1. In addition, the so far unknown absolute configuration of all three stereogenic centres of WF14861 could be established by this synthesis.

Kinetics and mechanism of the oxidation of some unsaturated acids by quinolinium bromochromate

The oxidation of maleic, fumaric, crotonic and cinnamic acids by quinolinium bromochromate (QBC) in dimethylsulphoxide (DMSO) leads to the formation of corresponding epoxide. The reaction is of first order with respect to QBC and the acid. The reaction is catalysed by hydrogen ions. The hydrogen-ion dependence has the form: kobs = a + b [H+]. The oxidation of these acids was studied in nineteen different organic solvents. The solvent effect was analyzed by Kamlet's and Swain's multiparametric equations. Solvent effect indicated the importance of the cation-solvating power of the solvent. A mechanism involving a three-centre transition state has been postulated.

Aza-peptide epoxides: A new class of inhibitors selective for clan CD cysteine proteases

Aza-peptide epoxides, a new class of irreversible protease inhibitors, are specific for the clan CD cysteine proteases. The inhibitors have second-order rate constants up to 105 M-1 s-1, with the most potent epoxides having the S,S stereochemistry. The aza-Asn derivatives are effective legumain inhibitors, while the aza-Asp epoxides were specific for caspases. The inhibitors have little or no inhibition with other proteases such as chymotrypsin, papain, or cathepsin B.

A stereocontrolled approach to electrophilic epoxides

Lithium t-butyl hydroperoxide (easily generated by addition of an alkyl-lithium to anhydrous t-butyl hydroperoxide in THF solution) is a powerful reagent for the epoxidation of electrophilic alkenes at -20 to 0 °C under full stereocontrol. Thus αβ-unsaturated esters, sulphones, sulphoximines, and amides are readily epoxidised with complete regio- and stereo-specificity and with considerable chiroselectivity (20-100%) when appropriate chiral auxiliaries such as menthyl, 8-phenylmenthyl, or a camphor-sulphonamide derivative are used. Asymmetric αβ-unsaturated sulphoximines undergo epoxidation with 100% diastereoselectivity. The only exceptions to stereocontrol noted are heavily substituted maleate esters such as di-t-butyl maleate. The αβ-epoxy amides are shown to be valuable sources of the corresponding epoxy ketones by treatment with an organolithium, allowing a stereo- and chemoselective entry in high yield to these useful intermediates.