80633-44-9

Upstream product

• 51-67-2 tyrosamine 
• 814-68-6 acryloyl chloride 

Downstream Products

• 20375-37-5 paprazine 
• 1260376-32-6 (E)-3-(3-bromo-4-methoxyphenyl)-N-(4-hydroxyphenethyl)acrylamide 
• 1260376-39-3 3,3-bis(3-bromo-4-methoxyphenyl)-N-(4-hydroxyphenethyl)acrylamide 
• 66648-43-9 (E)-N-feruloyltyramine 

Relevant academic research and scientific papers

The development of a general strategy for the synthesis of tyramine-based natural products by using continuous flow techniques

A flowing future! A multistep, general flow chemistry protocol has been developed for the preparation of tyramine-based natural products. The process integrates room-temperature reactions with high-temperature Heck coupling reactions, where the heat has been supplied by microwave irradiation. As a proof of concept for 'scaling out' to attain larger quantities of the desired products, the four primary tyramine-based natural products were prepared on a gram scale using this synthetic protocol.

Poly(n-acryl amino acids): A new class of biologically active polyanions

Poly(N-acryl amino acids) bearing side groups with a lipophilic character or having charged functional groups (i.e. -NH2, -COOH, -SH, -OH, and phenols) were synthesized from the radical polymerization of N-acryl amino acid monomers. Monomers were prepared from the reaction of acryloyl chloride and amino acid esters in dry solvents. Polymers of a broad molecular weight ranging from 3 000 to 60 000 Da were obtained. The polymers were optically active, and their structures were confirmed by 1H NMR and IR spectra and elemental analysis. Hydroxyl-containing polymers were sulfated in high conversion yields by SO3/pyridine complex. The newly synthesized linear homopolyanions were tested for heparin-like activities: (i) inhibition of heparanase enzyme, (ii) release of basic fibroblast growth factor (bFGF) from the extracellular matrix (ECM), and (iii) inhibition of smooth muscle cell (SMC) proliferation. Polymers based on tyrosine and leucine were highly active in all three tests (microgram level). Polymers based on phenylalanine, tert-leucine, and proline were active as heparanase inhibitors and FGF release, and polymers of trans-hydroxyproline, glycine, and serine were active only as heparanase inhibitors. The polymer of cis-hydroxyproline was inactive. It was found that a net anionic charge (i.e. carboxylic acid) is essential for biological activity. Thus, methyl ester derivatives of the active polymers, zwitterionic amino acid pendent groups (lysine, histidine), and decarboxylated amino acids (tyramine, ethanolamine) were inactive. The above active polymers did not exhibit anticoagulation activity which is considered the main limitation of heparin and heparinomimetics for clinical use. These synthetic poly(N-acryl amino acids) may have potential use in the inhibition of heparanase-mediated degradation of basement membranes associated with tumor metastasis, inflammation, and autoimmunity.

Custom-designed Glycopolymer Syntheses by Terpolymerizations

Carbohydrate derivatives having lectin binding properties and bearing N-acryloyl functionality have been copolymerized under three-component terpolymerization conditions with acrylamide and N-acryloylated effector molecules to provide water-soluble glycopolymers with custom designed physico-chemical properties.