127034-43-9

Basic information

• Product Name: (E)-3-(2-thienyl)-1-(3,4,5-trimethoxyphenyl)-3-phenylprop-2-en-1-one
• Synonyms: (E)-3-(2-thienyl)-1-(3,4,5-trimethoxyphenyl)-3-phenylprop-2-en-1-one
• CAS NO: 127034-43-9
• Molecular Weight: 304.367
• Mol File: 127034-43-9.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: (E)-3-(2-thienyl)-1-(3,4,5-trimethoxyphenyl)-3-phenylprop-2-en-1-one(CAS DataBase Reference)
• NIST Chemistry Reference: (E)-3-(2-thienyl)-1-(3,4,5-trimethoxyphenyl)-3-phenylprop-2-en-1-one(127034-43-9)
• EPA Substance Registry System: (E)-3-(2-thienyl)-1-(3,4,5-trimethoxyphenyl)-3-phenylprop-2-en-1-one(127034-43-9)

Safety Data

• Hazardous Substances Data: 127034-43-9(Hazardous Substances Data)

Upstream product

• 98-03-3 thiophene-2-carbaldehyde 
• 1136-86-3 methyl (3,4,5-trimethoxyphenyl) ketone 

Downstream Products

• 173543-10-7 [[1-(2-thienyl)-2-(3,4,5-trimethoxyphenyl)carbonyl-κO]ethenyl-κC(1)]tetracarbonylmanganese 

Relevant articles and documents

A novel series of benzothiazepine derivatives as tubulin polymerization inhibitors with anti-tumor potency

In this work, a series of diaryl benzo[b][1,4]thiazepine derivatives D1-D36 were synthesized and screened as tubulin polymerization inhibitors with anti-tumor potency. They were designed by introducing the seven-member ring benzothiazepine as the linker f

Synthetic compounds from an in house library as inhibitors of falcipain-2 from Plasmodium falciparum

Falcipain-2 (FP-2) is a key cysteine protease from the malaria parasite Plasmodium falciparum. Many previous studies have identified FP-2 inhibitors; however, none has yet met the criteria for an antimalarial drug candidate. In this work, we assayed an in-house library of non-peptidic organic compounds, including (E)-chalcones, (E)-N'-benzylidene-benzohydrazides and alkyl-esters of gallic acid, and assessed the activity toward FP-2 and their mechanisms of inhibition. The (E)-chalcones 48, 54 and 66 showed the lowest IC50 values (8.5±0.8μM, 9.5±0.2μM and 4.9±1.3μM, respectively). The best inhibitor (compound 66) demonstrated non-competitive inhibition, and using mass spectrometry and fluorescence spectroscopy assays, we suggest a potential allosteric site for the interaction of this compound, located between the catalytic site and the hemoglobin binding arm in FP-2. We combined structural biology tools and mass spectrometry to characterize the inhibition mechanisms of novel compounds targeting FP-2.