27282-86-6

Usage

Chemical structure

A triazine ring with two chlorine atoms and a cyclohexyl group attached

Type of compound

Derivative of triazine

Functional groups

Amine, dichloro, cyclohexyl

Applications

a. Intermediate in the synthesis of pharmaceuticals
b. Intermediate in the synthesis of agrochemicals
c. Potential applications in materials science

Hazardous nature

May be hazardous if not used properly

Safety precautions

Should be handled by individuals with appropriate training and protective equipment

Upstream product

• 108-77-0 1,3,5-trichloro-2,4,6-triazine 
• 108-91-8 cyclohexylamine 

Downstream Products

• 228574-87-6 C₁₅H₁₈ClN₅ 
• 1446756-52-0 C₁₀H₁₆ClN₅ 
• 1345866-14-9 C₉H₁₃ClN₄O 
• 32997-99-2 6-chloro-N⁽²⁾,N⁽⁴⁾-dicyclohexyl-1,3,5-triazine-2,4-diamine 
• 55338-67-5 N-cyclohexyl-4,6-dimethoxy-1,3,5-triazin-2-amine 

Relevant academic research and scientific papers

Synthesis and structure-activity relationship study of triazine-based inhibitors of the DNA binding of NF-κB

Nuclear transcription factor nuclear factor-kappa B (NF-κB) has diverse pathophysiological functions, and NF-κ B inhibitors are considered to be candidates for multiple therapeutic applications. We previously reported a novel triazine-based NF-κB inhibitor, 2-anilino-4,6-dichloro-1,3,5- triazine (NI241), that directly inhibits DNA binding of NF-κB. Here, we report synthesis of a series of triazine derivatives and evaluation of their structure-activity relationships for NF-κB inhibition. We found that 2-amino-4,6-dichloro-1,3,5-triazine substructure is essential for the inhibitory activity of the lead compound NI241, and modification of NI241 by introduction of an m-methoxy substituent on the phenyl ring afforded the more potent derivative 28. The structure-activity relationships identified in this study suggested a possible mechanism of irreversible NF-κB inhibition by NI241, and should be helpful in the design of other NF-κB inhibitors.

Straightforward synthesis of 2,4,6-trisubstituted 1,3,5-triazine compounds targeting cysteine cathepsins K and S

The synthesis and evaluation against various cysteine cathepsins with endopeptidase activity, of two new families of hitherto unknown 1,3,5-triazines, substituted by a nitrile function and either a cyclohexylamine moiety (5-like) or a piperazine moiety (9-like) are described. The structure-activity relationship was discussed; from 16 synthesized novel compounds, 9h was the most active and selectively inhibitor of Cat K (IC50 Combining double low line 28 nM) and Cat S (IC50 Combining double low line 23 nM). Molecular docking of 9h to X-ray crystal structure of cathepsins K and S confirmed a common binding mode with a crucial covalent bond with Cys25. We observed for 9h that p-trifluorophenyl group is located in S2 pocket and possess hydrophobic interactions with Tyr67 and Met68. Triazine and piperazine moieties are located in S′1 pocket and interact with Gly23, Cys63, Gly64 and Gly65. Altogether, these results indicate that the new analogs can make them effective agents against some viruses for which the glycoprotein cleavage is mediated by an array of proteases.

Compound with anti-aging and discoloration-resistant effects and preparation method thereof

The invention provides a compound with anti-aging and discoloration-resistant effects and a preparation method thereof. The compound has a structure shown as a formula (I), and in the formula, R, R1 and R2 are defined in the description. Compared with an

Trisubstituted 1,3,5-Triazines: The First Ligands of the sY12-Binding Pocket on Chemokine CXCL12

CXCL12, a CXC-type chemokine, binds its receptor CXCR4, and the resulting signaling cascade is essential during development and subsequently in immune function. Pathologically, the CXCL12-CXCR4 signaling axis is involved in many cancers and inflammatory diseases and thus has sparked continued interest in the development of therapeutics. Small molecules targeting CXCR4 have had mixed results in clinical trials. Alternatively, small molecules targeting the chemokine instead of the receptor provide a largely unexplored space for therapeutic development. Here we report that trisubstituted 1,3,5-triazines are competent ligands for the sY12-binding pocket of CXCL12. The initial hit was optimized to be more synthetically tractable. Fifty unique triazines were synthesized, and the structure-activity relationship was probed. Using computational modeling, we suggest key structural interactions that are responsible for ligand-chemokine binding. The lipophilic ligand efficiency was improved, resulting in more soluble, drug-like molecules with chemical handles for future development and structural studies.

Tailoring the Substitution Pattern on 1,3,5-Triazine for Targeting Cyclooxygenase-2: Discovery and Structure-Activity Relationship of Triazine-4-Aminophenylmorpholin-3-one Hybrids that Reverse Algesia and Inflammation in Swiss Albino Mice

Here, we report analgesic and anti-inflammatory activity of a series of compounds obtained by appending 4-aminophenylmorpholin-3-one and acyclic, cyclic, or heterocyclic moieties on 1,3,5-triazine. The structures of compounds 4b and 6b are optimized for the best inhibition of COX-2 with IC50 values of 0.06 and 0.08 μM, respectively, and selectivity over COX-1 of 166 and >125, respectively. At the dose of 5 mg kg-1, these compounds significantly reduced acetic acid induced writhings, and their ED50 values were found to be 2.2 and 1.9 mg kg-1, respectively. Besides the cell-based and animal-based experiments showing the modes of action of these compounds targeting COX-2, the interaction behavior of 4b with COX-2 was also characterized, with physicochemical experiments including ITC, NMR, UV-vis, and molecular-modeling studies. Characteristically, these compounds interact with R120, Y355, and W385, the residues responsible for holding the substrate and mediating the process of electron transfer during the metabolic phase of the enzyme.

Discovery of triazines as potent, selective and orally active PDE4 inhibitors

Expanding on HTS hit 4 afforded a series of [1,3,5]triazine derivatives as novel PDE4 inhibitors. The SAR development and optimization process with the emphasis on ligand efficiency and physicochemical properties led to the discovery of compound 44 as a potent, selective and orally active PDE4 inhibitor.

Synthesis of 4-amino-6-chloro-1,3,5-triazin-2(1H)-ones

Conditions for selective substitution for one chlorine atom in 2-(R,R-amino)-4,6-dichloro-1,3,5-triazines with a hydroxide ion were elaborated. Spectral and calculation methods showed that the products formed are in the lactam form, i.e., have the structure of 4-chloro-6-(R,R- amino)-1,3,5-triazin-2(1H)-ones.

Design, facile synthesis, antibacterial activity and structure-activity relationship of novel di- and tri-substituted 1,3,5-triazines

Due to overwhelming generation of drug resistant microorganisms, there is an urgent need to develop novel chemotherapeutic agents. In continuation of our research on discovery of novel heterocyclic scaffolds from 1,3,5-triazine, present study deals with design and development of some novel di- and tri-substituted 1,3,5-triazine derivatives. The synthesis of title analogues were accomplished by SNAr reaction and subsequently underwent rigorous antibacterial screening against a panel of representative Gram-negative and Gram-positive bacteria. Screening results revealed that minor structural variation may induce drastic changes in activity. Whereas, amine bridge and piprazine was termed as pivotal structural fragments necessary for generation and escalation of bio-activity. The structures of newly synthesized compounds were ascertained on the basis of their analytical and spectral profiles.

Identification and optimization of inhibitors of trypanosomal cysteine proteases: Cruzain, rhodesain, and TbCatB

Trypanosoma cruzi and Trypanosoma brucei are parasites that cause Chagas' disease and African sleeping sickness, respectively. Both parasites rely on essential cysteine proteases for survival: cruzain for T. cruzi and TbCatB/rhodesain for T. brucei. A rec

NOVEL SEH INHIBITORS AND THEIR USE

The invention is directed to novel sEH inhibitors and their use in the treatment of diseases mediated by the sEH enzyme.