223463-02-3

Basic information

• Product Name: 2-Amino-4-cyanopyridine
• Synonyms: (2,6-Dibromopyridin-4-yl)methanol;2,6-Dibromo-4-hydroxymethylpyridine
• CAS NO: 223463-02-3
• Molecular Formula: C₆H₅Br₂NO
• Molecular Weight: 266.93
• EINECS: -0
• Mol File: 223463-02-3.mol

Chemical Properties

• Melting Point: 110.0-111.5 °C
• Boiling Point: 379.7±37.0 °C(Predicted)
• Appearance: /
• Density: 2.071±0.06 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• PKA: 12.67±0.10(Predicted)
• CAS DataBase Reference: 2-Amino-4-cyanopyridine(CAS DataBase Reference)
• NIST Chemistry Reference: 2-Amino-4-cyanopyridine(223463-02-3)
• EPA Substance Registry System: 2-Amino-4-cyanopyridine(223463-02-3)

Safety Data

• Hazardous Substances Data: 223463-02-3(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
2-Amino-4-cyanopyridine is used as a chemical intermediate for the synthesis of various pharmaceuticals. Its unique structure allows for the development of new drugs with potential therapeutic benefits.
Used in Agrochemical Industry:
In the agrochemical sector, 2-Amino-4-cyanopyridine is utilized as a precursor in the production of pesticides and other agrochemicals, contributing to the development of effective solutions for crop protection.
Used in Dye Industry:
2-Amino-4-cyanopyridine is employed as a building block in the synthesis of dyes, enabling the creation of a wide range of colorants for various applications, including textiles, plastics, and printing inks.
Used in Cancer Research:
2-Amino-4-cyanopyridine has been studied for its potential use in the treatment of various diseases, particularly cancer. Its preclinical studies have shown promise in treating cancer, warranting further investigation into its therapeutic potential and possible incorporation into novel cancer treatment strategies.

Upstream product

• 408352-56-7 C-(2,6-dibromo-[4]pyridyl)-methylamine 
• 119308-57-5 methyl 2,6-dibromoisonicotinate 
• 90050-70-7 ethyl 2,6-dibromo-pyridine-4-carboxylate 
• 2016-99-1 2,6-dibromoisonicotinic acid 
• 99-11-6 citrazinic acid 
• 408352-58-9 2,6-dibromopyridine-4-carbonitrile 

Downstream Products

• 316800-46-1 2,6-Dibromopyridine-4-carbaldehyde 
• 108295-45-0 4′-formyl-2,2′:6′2″-terpyridine 
• 1431571-91-3 C₂₈H₁₈N₆ 
• 1148-79-4 2,2':6,2''-terpyridine 
• 408352-56-7 C-(2,6-dibromo-[4]pyridyl)-methylamine 

Relevant articles and documents

TYK-2 INHIBITOR

Disclosed herein is a compound of Formula (I) for inhibiting TYK2 and treating a disease associated with the undesirable tyk-2 activity (tyk-2 related diseases), a method of using the compounds disclosed herein for treating inflammatory or autoimmune disease, and a pharmaceutical composition comprising the same.

Rational Approach to Plasmonic Dimers with Controlled Gap Distance, Symmetry, and Capability of Precisely Hosting Guest Molecules in Hotspot Regions

Plasmonic dimers not only provide a unique platform for studying fundamental plasmonic behavior and effects but also are functional materials for numerous applications. The efficient creation of well-defined dimers with flexible control of structure parameters and thus tunable optical property is the prerequisite for fully exploiting the potential of this nanostructure. Herein, based on a polymer-assisted self-assembly approach in conjugation with molecular cage chemistry, a strategy was demonstrated for constructing cage-bridged plasmonic dimers with controlled sizes, compositions, shape, symmetry, and interparticle gap separation in a modular and high-yield manner. With a high degree of freedom and controllability, this strategy allows facilely accessing various symmetrical/asymmetrical dimers with sub-5 nm gap distance and tailored optical properties. Importantly, as the linkage of the two constituent elements, the molecular cages embedded in the junction endow the assembled dimers with the ability to precisely and reversibly host rich guest molecules in hotspot regions, offering great potential for creating various plasmon-mediated applications.

Protein-Induced Change in Ligand Protonation during Trypsin and Thrombin Binding: Hint on Differences in Selectivity Determinants of Both Proteins?

Trypsin and thrombin, structurally similar serine proteases, recognize different substrates; thrombin cleaves after Arg, whereas trypsin cleaves after Lys/Arg. Both recognize basic substrate headgroups via Asp189 at the bottom of the S1 pocket. By crystal

PYRIDYL OR PYRIMIDYL MTOR KINASE INHIBITORS

The invention relates to compounds or pharmaceutically acceptable salts thereof of formula (I): (I) wherein R1, R2, R3, R4, R4' and R5 are as defined in the description and claims; and comp

2 Tyrosine kinase mediated signal transduction inhibitors

Disclosed herein are compounds of Formula (), and pharmaceutically acceptable salts thereof, wherein R, R, R, R, R, X, X, X, X, X, and n are as defined herein, pharmaceutical compositions comprising same, and methods of preparation and use.

Attachment of a RuII Complex to a Self-Folding Hexaamide Deep Cavitand

We report the design, synthesis and characterization of a new RuII metallocavitand that is catalytically active in alkene epoxidation reactions. The elaboration of the resorcin[4]arene's aromatic cavity produced a self-folding, deep hexaamide cavitand featuring a single diverging terpyridine (tpy) group installed at its upper rim. The construction of the metallocavitand involved the initial chelation of a RuIII chloride complex by the tpy ligand followed by the incorporation of 2-(phenylazo)pyridine (azpy) as an ancillary ligand. The resulting RuII chloro complex was converted into the catalytically active aqua counterpart by a ligand exchange process.

First Structure-Activity Relationship of 17β-Hydroxysteroid Dehydrogenase Type 14 Nonsteroidal Inhibitors and Crystal Structures in Complex with the Enzyme

17β-HSD14 belongs to the SDR family and oxidizes the hydroxyl group at position 17 of estradiol and 5-androstenediol using NAD+ as cofactor. The goal of this study was to identify and optimize 17β-HSD14 nonsteroidal inhibitors as well as to disclose their structure-activity relationship. In a first screen, a library of 17β-HSD1 and 17β-HSD2 inhibitors, selected with respect to scaffold diversity, was tested for 17β-HSD14 inhibition. The most interesting hit was taken as starting point for chemical modification applying a ligand-based approach. The designed compounds were synthesized and tested for 17β-HSD14 inhibitory activity. The two best inhibitors identified in this study have a very high affinity to the enzyme with a Ki equal to 7 nM. The strong affinity of these inhibitors to the enzyme active site could be explained by crystallographic structure analysis, which highlighted the role of an extended H-bonding network in the stabilization process. The selectivity of the most potent compounds with respect to 17β-HSD1 and 17β-HSD2 is also addressed.

Inhibition of cancer-associated mutant isocitrate dehydrogenases: Synthesis, structure-activity relationship, and selective antitumor activity

Mutations of isocitrate dehydrogenase 1 (IDH1) are frequently found in certain cancers such as glioma. Different from the wild-type (WT) IDH1, the mutant enzymes catalyze the reduction of α-ketoglutaric acid to d-2-hydroxyglutaric acid (D2HG), leading to cancer initiation. Several 1-hydroxypyridin-2-one compounds were identified to be inhibitors of IDH1(R132H). A total of 61 derivatives were synthesized, and their structure-activity relationships were investigated. Potent IDH1(R132H) inhibitors were identified with Ki values as low as 140 nM, while they possess weak or no activity against WT IDH1. Activities of selected compounds against IDH1(R132C) were found to be correlated with their inhibitory activities against IDH1(R132H), as well as cellular production of D2HG, with R2 of 0.83 and 0.73, respectively. Several inhibitors were found to be permeable through the blood-brain barrier in a cell-based model assay and exhibit potent and selective activity (EC50 = 0.26-1.8 μM) against glioma cells with the IDH1 R132H mutation.

Thiol-ene reaction: A versatile tool in site-specific labelling of proteins with chemically inert tags for paramagnetic NMR

Site-specific tagging of proteins with paramagnetic lanthanides generates valuable long-range structure restraints for structural biology by NMR spectroscopy. We show that the thiol-ene addition reaction offers a powerful tool for tagging proteins in a chemically stable manner with very small lanthanide tags. The Royal Society of Chemistry 2012.

Online monitoring of hydroformylation intermediates by ESI-MS

Self-assembling ligands bearing permanently charged moieties have been synthesized and investigated in the Rh-catalyzed hydroformylation of terminal alkenes. By coupling a high-pressure autoclave directly to an ESI mass spectrometer hydroformylation reactions applying self-assembling 6-DPPon ligands could be studied in an online fashion. The live-streaming of the reaction mixture to the spectrometer revealed a series of different complexes not observed by other methods before, the structures of which were corroborated by CID experiments. Under CO/H2 atmosphere, new complexes that are predicted by the Wilkinson catalytic cycle could be identified and studied by CID experiments, too. Especially the ion at m/z 848, a square-planar hydrido-carbonyl complex that is normally not detectable by other methods, was investigated in detail. Collision experiments of this complex resulted in the loss of CO and H2, the latter being quite unusual, and points to the involvement of the hydrogen bond framework. These findings were further supported by deuteration experiments that revealed a clear incorporation of deuterium into the ligands. From these findings a new hydrogen-activation mechanism was proposed. Furthermore, substrate-containing complexes could be generated too, though a huge excess of substrate was necessary. CID experiments either with D2 or Ar yielded nearly identical spectra, hinting at a complex that might result either from a β-hydride elimination or from intramolecular oxidative addition of one of the ligands.