17087-75-1

Upstream product

• 165877-67-8 (+)(2R:3R)-3-chloro-2-hydroxy-succinic acid 
• 141-36-6 DL-trans-epoxysuccinic acid 
• 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 
• 3291-46-1 (2SR,3SR)-oxirane-2,3-dicarboxylic acid diethyl ester 
• 624-49-7 dimethylfumarate 
• 75-91-2 tert.-butylhydroperoxide 
• 3291-46-1 (2S,3S)-diethyl oxirane-2,3-dicarboxylate 
• 3272-11-5 2,3-oxiranedicarboxylic acid 

Downstream Products

• 141-36-6 DL-trans-epoxysuccinic acid 
• 22734-81-2 trans-epoxysuccinyl chloride 
• 1631180-15-8 C₂₆H₃₈N₆O₁₁ 
• 17087-75-1 (-)-trans-2,3-oxiranedicarboxylic acid 
• 17015-08-6 (2R,3R)-oxirane-2,3-dicarboxylic acid 
• 16417-32-6 N-benzyl-erythro-β-hydroxy-DL-aspartic acid 
• 3291-46-1 (2SR,3SR)-oxirane-2,3-dicarboxylic acid diethyl ester 
• 3291-46-1 (2S,3S)-diethyl oxirane-2,3-dicarboxylate 
• 133-37-9 DL-tartaric acid 
• 75-07-0 acetaldehyde 
• 87-69-4 tartaric acid 
• 1186-90-9 erythro-β-hydroxy-DL-aspartic acid 
• 6463-75-8 N-(DL-α-Methyl-benzyl)-erythro-β-hydroxy-DL-asparaginsaeure 
• 646532-92-5 (2S,3S)-oxirane-2,3-dicarboxylic acid monobenzyl ester 

Relevant academic research and scientific papers

2,3-EPOXY SUCCINYL DERIVATIVE, PREPARATION METHOD THEREFOR, AND USES THEREOF

The present invention relates to a 2,3-epoxy succinyl derivative, a preparation method and a use thereof, in particular, the present invention relates to a compound represented by Formula (1), a racemate or an optical isomer thereof, a solvate thereof, or

Design, synthesis, and structure–activity relationship study of epoxysuccinyl–peptide derivatives as cathepsin B inhibitors

Cathepsin B is a lysosomal cysteine protease involved in many diseases. The present research demonstrates that derivatives of epoxysuccinyl–peptide are effective and selective cathepsin B inhibitors. We synthesized a series of epoxysuccinyl–peptide deriva

2, 3-Butanediamide Epoxide Compound and Preparation Method and Use Thereof

Provided are a compound of formula I which can be used as a drug against small RNA virus infections, and optical isomers, pharmaceutically acceptable salts, solvates or hydrates thereof. Also provided are the preparation method of the compound, the method for using the compound for treating bacterial infections and the use of the compound in the preparation of a drug for preventing and/or treating viral diseases caused by small RNA viruses.

Probing of primed and unprimed sites of calpains: Design, synthesis and evaluation of epoxysuccinyl-peptide derivatives as selective inhibitors

Calpains are intracellular cysteine proteases with important physiological functions. Up- or downregulation of their expression can be responsible for several diseases, therefore specific calpain inhibitors may be considered as promising candidates for drug discovery. In this paper we describe the synthesis and characterization of a new class of inhibitors derived from the analysis of amino acid preferences in primed and unprimed sites of calpains by incorporation of l- or d-epoxysuccinyl group (Eps). Amino acids for replacement were chosen by considering the substrate preference of calpain 1 and 2 enzymes. The compounds were characterized by RP-HPLC, amino acid analysis and ESI-MS. Selectivity of the compounds was studied by using calpain 1 and 2; and cathepsin B. We have identified five calpain specific inhibitors with different extent of selectivity. Two of these also exhibited isoform selectivity. Compound NH 2-Thr-Pro-Leu-(d-Eps)-Thr-Pro-Pro-Pro-Ser-NH2 proved to be a calpain 2 enzyme inhibitor with at least 11.8-fold selectivity, while compound NH2-Thr-Pro-Leu-(l-Eps)-Ser-Pro-Pro-Pro-Ser-NH2 possesses calpain 1 enzyme inhibition with at least 4-fold selectivity. The results of molecular modeling calculations suggest that the orientation of the bound inhibitor in the substrate binding cleft is markedly dependent on the stereochemistry of the epoxysuccinyl group.

Design, synthesis, and screen of cathepsin K inhibitors

We synthesized a series of epoxysuccinic acid derivatives and evaluated their in vitro cathepsin K inhibitory activity The screening results show that the potency of compounds 9e, 9d, 9p, 9j and 9k (IC50 ≤ 0.005 μmol/L) were equal to or greater than that of the lead compound 9a. Less hydrophobic compounds showed weaker potency, which can be explained by the hydrophobic nature of the cathepsin K binding pockets.

EPOXY-CONTAINING POLY(ESTER AMIDES) AND METHODS OF USE

The invention provides aliphatic epoxy-containing PEA polymer compositions with film-forming properties. The aliphatic epoxy di-acids used in the invention PEA compositions include non-toxic fatty aliphatic epoxy homologs. A second, C-protected L-lysine-based monomer can be introduced into the polymer to provide additional chain flexibility. The invention PEA polymer compositions are useful for delivery of bioactive agents when administered internally or used in the manufacture of implantable medical devices. Biodegradable hydrogels can be made using the invention epoxy-containing PEAs.

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.