685543-77-5

Basic information

• Product Name: 3-BENZYLCARBAMOYL-ACRYLIC ACID
• Synonyms: 3-BENZYLCARBAMOYL-ACRYLIC ACID
• CAS NO: 685543-77-5
• Molecular Formula: C₁₁H₁₁NO₃
• Molecular Weight: 205.21
• Mol File: 685543-77-5.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 3-BENZYLCARBAMOYL-ACRYLIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: 3-BENZYLCARBAMOYL-ACRYLIC ACID(685543-77-5)
• EPA Substance Registry System: 3-BENZYLCARBAMOYL-ACRYLIC ACID(685543-77-5)

Safety Data

• Hazardous Substances Data: 685543-77-5(Hazardous Substances Data)

Upstream product

• 108-31-6 maleic anhydride 
• 100-46-9 benzylamine 
• 627-63-4 fumaryl dichloride 
• 110-17-8 (2E)-but-2-enedioic acid 
• 2459-05-4 (E)-4-ethoxy-4-oxobut-2-enoic acid 
• 26367-48-6 fumaric acid ethyl ester mono chloride 
• 474024-61-8 4-oxo-4-[(phenylmethyl)amino]-(E)-2-butenoic acid ethyl ester 

Downstream Products

• 25800-55-9 N²,N⁴-dibenzyl-asparagine 
• 685543-82-2 4-{1-[N'-(3-benzylcarbamoyl-acryloyl)-N'-tert-butoxycarbonylmethyl-hydrazinocarbonyl]-2-methyl-propylcarbamoyl}-4-(2-benzyloxycarbonylamino-3-tert-butoxycarbonyl-propionylamino)-butyric acid tert-butyl ester 

Relevant articles and documents

Aza-peptidyl michael acceptor and epoxide inhibitors - Potent and selective inhibitors of Schistosoma mansoni and Ixodes ricinus legumains (asparaginyl endopeptidases)

Aza-peptide Michael acceptors and epoxides with the general structure of YCO-Ala-Ala-AAsn-trans-CH=CHCOR and YCO-Ala-Ala-AAsn-EP-COR, respectively, are shown to be potent inhibitors of asparaginyl endopeptidases (legumains) from the bloodfluke, Schistosoma mansoni (SmAE), and the hard tick, Ixodes ricinus (IrAE). Structure-activity relationships (SARs) were determined for a set of 41 aza-peptide Michael acceptors and eight aza-peptide epoxides. Both enzymes prefer disubstituted amides to monosubstituted amides in the P10 position, and potency increased as we increased the hydrophobicity of the inhibitor in this position. Extending the inhibitor to P5 resulted in increased potency, especially against IrAE, and both enzymes prefer small over large hydrophobic residues at P2. Aza-peptide Michael acceptor inhibitors are more potent than aza-peptide epoxide inhibitors, and for some of these compounds, second-order inhibiton rate constants are the fastest yet discovered. Given the central functions of these enzymes in both parasites, the data presented here may facilitate the eventual design of selective antiparasitic drugs.

Chemospecific allylation and domino metathesis of 7-oxanorbornenes for skeletal and appendage diversity

We report a synthetic strategy for skeletally diverse heterocycles featuring appendage diversity based on a tandem Ugi/ Diels-Alder reaction followed by domino metathesis. An associating effect of the amide carbonyl functionality to the ruthenium metal ce

Aza-peptidyl Michael acceptors. A new class of potent and selective inhibitors of asparaginyl endopeptidases (legumains) from evolutionarily diverse pathogens

Aza-peptide Michael acceptors with the general structure of Cbz-Ala-Ala-AAsn-trans-CH=CHCOR are a new class of inhibitors specific for the asparaginyl endopeptidases (AE) (legumains). Structure-activity relationships (SARs) were characterized for a set of 31 aza-peptide Michael acceptors with AEs derived from three medically important parasites: the protist Trichomonas vaginalis, the hard tick Ixodes ricinus, and the flatworm Schistosoma mansoni. Despite arising from phylogenetically disparate organisms, all three AEs shared a remarkably similar SAR with lowest IC50 values extending into the picomolar range. The results suggest an evolutionary constraint on the topography of the prime side of the active site. SAR also revealed that esters in the P1′ position are more potent than disubstituted amides and that monosubstituted amides and alkyl derivatives show little or no inhibition. The preferred P1′ residues have aromatic substituents. Aza-asparaginyl Michael acceptors react with thiols, which provides insight into the mechanism of their inhibition of asparaginyl endopeptidases.

Design, synthesis, and evaluation of aza-peptide Michael acceptors as selective and potent inhibitors of caspases-2, -3, -6, -7, -8, -9, and -10

Aza-peptide Michael acceptors are a novel class of inhibitors that are potent and specific for caspases-2, -3, -6, -7, -8, -9, and -10. The second-order rate constants are in the order of 106 M-1 s-1. The aza-peptide Michael acceptor inhibitor 18t (Cbz-Asp-Glu-Val-AAsp-trans-CH=CH-CON(CH2-1-Naphth)2 is the most potent compound and it inhibits caspase-3 with a k2 value of 5620000 M-1 s-1. The inhibitor 18t is 13700, 190, 6.4, 594, 37500, and 173-fold more selective for caspase-3 over caspases-2, -6, -7, -8, -9, and -10, respectively. Aza-peptide Michael acceptors designed with caspase specific sequences are selective and do not show any cross reactivity with clan CA cysteine proteases such as papain, cathepsin B, and calpains. High-resolution crystal structures of caspase-3 and caspase-8 in complex with aza-peptide Michael acceptor inhibitors demonstrate the nucleophilic attack on C2 and provide insight into the selectivity and potency of the inhibitors with respect to the P1′ moiety.

Parallel synthesis of tandem Ugi/Diels-Alder reaction products on a soluble polymer support directed toward split-pool realization of a small molecule library

A hundred reactions were demonstrated on the soluble MPEG-O-CH 2-platform. The reaction can be also effected on insoluble TentaGel resin using the same linker. A series of parallel reactions were carried out for the tandem Ugi/Diels-Alder reaction on our MPEG-O-CH2- platform. Ninety-six out of a 100 entries were successful to give complex heterotricycles. The stereoselectivity was found not to be influenced by the building blocks used for amine and carboxylic acid components. An unexpected side pathway was found but was suppressed by employing appropriate reaction conditions. The reaction was also performed on solid phase, by which a larger library is potentially realized by employing the split-pool method.

PROPENOYL HYDRAZIDES

The present disclosure provides compositions for inhibiting proteases, methods for synthesizing the compositions, and methods of using the disclosed protease inhibitors. Aspects of the disclosure include a peptidyl propenoyl hydrazide compositions that inhibit proteases, for example cysteine proteases, either in vivoor in vitro.

Aza-Peptide Michael Acceptors: A New Class of Inhibitors Specific for Caspases and Other Clan CD Cysteine Proteases

Aza-peptide Michael acceptors are a new class of irreversible inhibitors that are highly potent and specific for clan CD cysteine proteases. The aza-Asp derivatives were specific for caspases, while aza-Asn derivatives were effective legumain inhibitors. Aza-Lys and aza-Orn derivatives were potent inhibitors of gingipain K and clostripain. Aza-peptide Michael acceptors showed no cross reactivity toward papain, cathepsin B, and calpain.