73428-20-3

Upstream product

• 51-67-2 tyrosamine 
• 90-02-8 salicylaldehyde 
• 89-95-2 2-methyl-benzyl alcohol 
• 60-19-5 tyramine hydrochloride 
• 932-30-9 2-Hydroxybenzylamine 

Relevant academic research and scientific papers

Inclusion of Peripheral Basic Groups Activates Dormant Cobalt-Based Molecular Complexes for Catalytic H2 Evolution in Water

The protein scaffold plays a key role during the enzymatic catalysis for metalloenzymes. Here we have rationally designed an enzyme-inspired outer coordination sphere in the form of protic functionalities, such as natural amino acid derived carboxylic acid and phenolic -OH groups, on the fringe of the cobalt-salen like complexes. This inclusion has enabled electrocatalytic H2 evolution for an otherwise inactive cobalt-salen like core. The complexes containing peripheral carboxylic acid groups exhibited unique pH-switchable catalytic H2 production that is connected with the pKa of the carboxylic acid group (～4.0), suggesting the crucial involvement of the carboxylate group during the catalytic activity. The one- and two-dimensional NMR results of the complexes have indicated the presence of a possible hydrogen bonding network, generated by those protic groups in aqueous solution. These results highlight that an inactive metal complex can be activated for specific small molecule activation via rational inclusion of outer coordination sphere functionalities.

Effect of N, N Coordination and RuII Halide Bond in Enhancing Selective Toxicity of a Tyramine-Based RuII (p-Cymene) Complex

Ruthenium compounds are promising anticancer candidates owing to their lower side-effects and encouraging activities against resistant tumors. Half-sandwich piano-stool type RuII compounds of general formula [(L)RuII(η6-arene)(X)]+ (L = chelating bidentate ligand, X = halide) have exhibited significant therapeutic potential against cisplatin-resistant tumor cell lines. In RuII (p-cymene) based complexes, the change of the halide leaving group has led to several interesting features, viz., hydrolytic stability, resistance toward thiols, and alteration in pathways of action. Tyramine is a naturally occurring monoamine which acts as a catecholamine precursor in humans. We synthesized a family of N,N and N,O coordinated RuII (p-cymene) complexes, [(L)RuII(η6-arene)(X)]+ (1-4), with tyramine and varied the halide (X = Cl, I) to investigate the difference in reactivity. Our studies showed that complex 2 bearing N,N coordination with an iodido leaving group shows selective in vitro cytotoxicity against the pancreatic cancer cell line MIA PaCa-2 (IC50 ca. 5 μM) but is less toxic to triple-negative breast cancer (MDA-MB-231), hepatocellular carcinoma (Hep G2), and the normal human foreskin fibroblasts (HFF-1). Complex 2 displays stability toward hydrolysis and does not bind with glutathione, as confirmed by 1H NMR and ESI-HRMS experiments. The inert nature of 2 leads to enhancement of cytotoxicity (IC50 = 5.3 ± 1 μM) upon increasing the cellular treatment time from 48 to 72 h.

spiro-Cyclotriphosphazenes containing 4-hydroxyphenylethyl pendant arm: Syntheses, structural characterization and DNA interaction study

The reaction of hexachlorocyclotriphosphazene, N3P3Cl6, with tyramine podand (2) afforded partly substituted spiro-cyclotriphosphazene (3). Amine-substituted spiro-cyclotriphosphazenes 4a–g were prepared by substitution of

Ultrasonic synthesis of tyramine derivatives as novel inhibitors of α-glucosidase in vitro

Tyramine derivatives 3–27 were synthesized by using conventional and environmental friendly ultrasonic techniques. These derivatives were then evaluated for the first time for their α-glucosidase (Sources: Saccharomyces cerevisiae and mammalian rat-intest

ABSCISIC ACID BIOSYNTHESIS INHIBITOR

Compounds represented by the following general formula (I) or salts thereof: wherein R1 represents hydrogen atom, hydroxyl group, or an alkoxy group; R2 represents hydroxyl group or an alkoxy group which may be substituted; R3/

A new lead compound for abscisic acid biosynthesis inhibitors targeting 9-cis-epoxycarotenoid dioxygenase

9-cis-Epoxycarotenoid dioxygenase (NCED), a key enzyme in abscisic acid (ABA) biosynthesis, cleaves the olefinic double bond of 9-cis-epoxycarotenoid. Several analogues of nordihydroguaiaretic acid (NDGA) were designed and synthesized, and their efficacy