28028-86-6

Upstream product

• 14371-10-9 (E)-3-phenylpropenal 
• 141-82-2 malonic acid 
• 7664-93-9 sulfuric acid 
• 108-24-7 acetic anhydride 
• 104-55-2 3-phenyl-propenal 
• 17041-60-0 dimethyl ethylidenemalonate 
• 100-52-7 benzaldehyde 

Downstream Products

• 94879-87-5 (+/-)-5-trans-cinnamylidene-2-trans-styryl-[1,3]dioxane-4,6-dione 
• 5454-06-8 3-phenylpropylmalonic acid 
• 100315-79-5 (3-cyclohexyl-propyl)-malonic acid 
• 28010-12-0 5-phenylpenta-2,4-dienoic acid 
• 1552-94-9 (2Z,4E)-5-phenylpenta-2,4-dienoic acid 
• 5962-88-9 5-cyclohexylvaleric acid 

Relevant academic research and scientific papers

2u202f+u202f2 Dimerization of cinnamylidene malonic acid: A structural and kinetic study

Cinnamylidene malonic acid was synthesized and its crystal structure obtained. The dicarboxylic acid hydrogen-bonding motif of this structure consists of catemer chains that lie along the c- glide plane. A photo induced 2 + 2 cycloaddition occurred upon exposure of the crystals to UV light which resulted in the destruction of the crystal. The structure of the photo products were determined by IR and NMR analysis. The regio- and stereo-chemistry of the photoproduct can be rationalized by examining the relative orientation and symmetry relating reacting molecules within the crystal structure. A kinetic study demonstrated first order reaction kinetics which is consistent with a reaction occurring under topochemical control.

Identification of cinnamic acid derivatives as novel antagonists of the prokaryotic proton-gated ion channel GLIC

Pentameric ligand gated ion channels (pLGICs) mediate signal transduction. The binding of an extracellular ligand is coupled to the transmembrane channel opening. So far, all known agonists bind at the interface between subunits in a topologically conserved "orthosteric site" whose amino acid composition defines the pharmacological specificity of pLGIC subtypes. A striking exception is the bacterial proton-activated GLIC protein, exhibiting an uncommon orthosteric binding site in terms of sequence and local architecture. Among a library of Gloeobacter violaceus metabolites, we identified a series of cinnamic acid derivatives, which antagonize the GLIC proton-elicited response. Structure-activity analysis shows a key contribution of the carboxylate moiety to GLIC inhibition. Molecular docking coupled to site-directed mutagenesis support that the binding pocket is located below the classical orthosteric site. These antagonists provide new tools to modulate conformation of GLIC, currently used as a prototypic pLGIC, and opens new avenues to study the signal transduction mechanism.

A tentative descriptive modelling of chemical structure-biological activity relationships. Biological evaluation of a series of polyethylenic acids

48 new polyethylenic-malonic acids have been submitted to an antimicrobial and antifungal screening. After a suitable recoding, the experimental results were analyzed according to two mathematical multivariate analysis using a computer process i.e. Correspondence Factorial Analysis and Cluster Analysis. These methods allowed an accurate study of the structure of the system and a thorough investigation of the structure-activity-specificity relationships. On the other side, magnitude and/or specificity of the observed biological effects were related to structural features. These results should be useful in order to elaborate synthetic strategies.