881-86-7

Usage

Uses

Used in Pharmaceutical Industry:
DIMETHYL PYRIDINE-2,5-DICARBOXYLATE is used as an intermediate in the synthesis of potent antitumor agents. Its unique chemical structure allows it to be a key component in the development of new and effective cancer treatments.
Used in Chemical Synthesis:
DIMETHYL PYRIDINE-2,5-DICARBOXYLATE is used as a versatile intermediate in the synthesis of various organic compounds. Its reactivity and functional groups make it suitable for a wide range of chemical reactions, contributing to the production of different chemical products.
General Description:
DIMETHYL PYRIDINE-2,5-DICARBOXYLATE can be prepared from 2,5-pyridinedicarboxylic acid through a series of chemical reactions. Its synthesis involves the esterification of the carboxylic acid groups, resulting in the formation of the dimethyl ester. DIMETHYL PYRIDINE-2,5-DICARBOXYLATE serves as a crucial building block in the development of new pharmaceuticals and other chemical products.

InChI:InChI=1/C9H9NO4/c1-13-8(11)6-3-4-7(10-5-6)9(12)14-2/h3-5H,1-2H3

Upstream product

• 3222-47-7 6-methylnicotinic acid 
• 67-56-1 methanol 
• 100-26-5 Pyridine-2,5-dicarboxylic acid 
• 16110-09-1 2,5 dichloropyridine 
• 201230-82-2 carbon monoxide 
• 624-28-2 2,5-dibromopyridine 
• 485-80-3 S-adenosyl-L-methionine 
• 589-93-5 2,5-dimethylpyridine 
• 186581-53-3 diazomethane 
• 136-45-8 dipropyl pyridine-2,5-dicarboxylate 
• 74-88-4 methyl iodide 

Downstream Products

• 4663-96-1 pyridine-2,5-dicarboxylic acid diamide 
• 2207-52-5 piperidine-2,5-dicarboxylic acid dimethyl ester 
• 512782-63-7 6-hydrazinocarbonyl-nicotinic acid methyl ester 
• 6011-55-8 2,5-pyridinedicarboxylic dihydrazide 
• 117517-54-1 methyl 6-carbamoylnicotinate 
• 56026-36-9 methyl 6-(hydroxymethyl)nicotinate 
• 170464-32-1 6-(methylcarbamoyl)pyridine-3-carboxylic acid 
• 145012-49-3 5-(methoxycarbonyl)piperidine-2-carboxylic acid 
• 37877-95-5 [2](1,4)benzeno[2](2,5)pyridinophane 
• 288083-60-3 6-dimethylcarbamoyl-nicotinic acid 
• 20857-31-2 ethyl 6-formyl-pyridine-3-carboxylate 
• 40749-33-5 5-(hydroxymethyl)-2-pyrimidinecarboxaldehyde 
• 2207-52-5 cis-2,5-Piperidinedicarboxylic acid methyl ester 
• 117517-48-3 methyl 2-phenylaminocarbonylpyridine-5-carboxylate 

Relevant academic research and scientific papers

Carboxyl Methyltransferase Catalysed Formation of Mono- and Dimethyl Esters under Aqueous Conditions: Application in Cascade Biocatalysis

Carboxyl methyltransferase (CMT) enzymes catalyse the biomethylation of carboxylic acids under aqueous conditions and have potential for use in synthetic enzyme cascades. Herein we report that the enzyme FtpM from Aspergillus fumigatus can methylate a broad range of aromatic mono- and dicarboxylic acids in good to excellent conversions. The enzyme shows high regioselectivity on its natural substrate fumaryl-l-tyrosine, trans, trans-muconic acid and a number of the dicarboxylic acids tested. Dicarboxylic acids are generally better substrates than monocarboxylic acids, although some substituents are able to compensate for the absence of a second acid group. For dicarboxylic acids, the second methylation shows strong pH dependency with an optimum at pH 5.5–6. Potential for application in industrial biotechnology was demonstrated in a cascade for the production of a bioplastics precursor (FDME) from bioderived 5-hydroxymethylfurfural (HMF).

Development of Gene-Targeted Polypyridyl Triplex-Forming Oligonucleotide Hybrids

In the field of nucleic acid therapy there is major interest in the development of libraries of DNA-reactive small molecules which are tethered to vectors that recognize and bind specific genes. This approach mimics enzymatic gene editors, such as ZFNs, TALENs and CRISPR-Cas, but overcomes the limitations imposed by the delivery of a large protein endonuclease which is required for DNA cleavage. Here, we introduce a chemistry-based DNA-cleavage system comprising an artificial metallo-nuclease (AMN) that oxidatively cuts DNA, and a triplex-forming oligonucleotide (TFO) that sequence-specifically recognises duplex DNA. The AMN-TFO hybrids coordinate CuII ions to form chimeric catalytic complexes that are programmable – based on the TFO sequence employed – to bind and cut specific DNA sequences. Use of the alkyne-azide cycloaddition click reaction allows scalable and high-throughput generation of hybrid libraries that can be tuned for specific reactivity and gene-of-interest knockout. As a first approach, we demonstrate targeted cleavage of purine-rich sequences, optimisation of the hybrid system to enhance stability, and discrimination between target and off-target sequences. Our results highlight the potential of this approach where the cutting unit, which mimics the endonuclease cleavage machinery, is directly bound to a TFO guide by click chemistry.

A cationic Zr-based metal organic framework with enhanced acidic resistance for selective and efficient removal of CrO42-

Water pollution caused by CrO42- has become a global concern due to its high aqueous solubility and good mobility in the underground environment. Recently, water stable zirconium based metal-organic frameworks (Zr-MOFs) have been tested as adsorbents to remove pollutants from contaminated water. However, the low adsorption capacity of Zr-MOFs towards ionic pollutants is unsatisfactory due to their neutral nature. Herein, a cationic Zr-MOF (Zr-C-MOF) was obtained by directly introducing a pyridinium salt as a ligand with an impressive ion exchange capability. Zr-C-MOF demonstrated enhanced acidic resistance and selectively high adsorption of CrO42-. The characteristics of the obtained Zr-C-MOF were confirmed via various techniques including PXRD, FT-IR spectroscopy, 1H-NMR spectroscopy, TGA, SEM, EDX and XPS. Batch adsorption studies have been conducted to gain a deep understanding of the kinetics mechanism, pH effects, adsorption isotherm and the effects of other competing ions. The kinetics and adsorption isotherm of CrO42- adsorption onto Zr-C-MOF were found to well fit the pseudo-second-order rate equation and the Langmuir model, respectively. The comparison of FT-IR, PXRD, SEM, EDX and XPS results of the samples before and after CrO42- adsorption revealed the adsorption mechanism of the anion exchange process. This journal is

Design, synthesis, and biological characterization of a new class of symmetrical polyamine-based small molecule CXCR4 antagonists

CXCR4, a well-studied coreceptor of human immunodeficiency virus type 1 (HIV-1) entry, recognizes its cognate ligand SDF-1α (also named CXCL12) which plays many important roles, including regulating immune cells, controlling hematopoietic stem cells, and directing cancer cells migration. These pleiotropic roles make CXCR4 an attractive target to mitigate human disorders. Here a new class of symmetrical polyamines was designed and synthesized as potential small molecule CXCR4 antagonists. Among them, a representative compound 21 (namely HF50731) showed strong CXCR4 binding affinity (mean IC50 = 19.8 nM) in the CXCR4 competitive binding assay. Furthermore, compound 21 significantly inhibited SDF-1α-induced calcium mobilization and cell migration, and blocked HIV-1 infection via antagonizing CXCR4 coreceptor function. The structure-activity relationship analysis, site-directed mutagenesis, and molecular docking were conducted to further elucidate the binding mode of compound 21, suggesting that compound 21 could primarily occupy the minor subpocket of CXCR4 and partially bind in the major subpocket by interacting with residues W94, D97, D171, and E288. Our studies provide not only new insights for the fragment-based design of small molecule CXCR4 antagonists for clinical applications, but also a new and effective molecular probe for CXCR4-targeting biological studies.

New Water-Soluble Copper(II) Complexes with Morpholine-Thiosemicarbazone Hybrids: Insights into the Anticancer and Antibacterial Mode of Action

Six morpholine-(iso)thiosemicarbazone hybrids HL1-HL6 and their Cu(II) complexes with good-to-moderate solubility and stability in water were synthesized and characterized. Cu(II) complexes [Cu(L1-6)Cl] (1-6) formed weak dimeric associates in the solid state, which did not remain intact in solution as evidenced by ESI-MS. The lead proligands and Cu(II) complexes displayed higher antiproliferative activity in cancer cells than triapine. In addition, complexes 2-5 were found to specifically inhibit the growth of Gram-positive bacteria Staphylococcus aureus with MIC50 values at 2-5 μg/mL. Insights into the processes controlling intracellular accumulation and mechanism of action were investigated for 2 and 5, including the role of ribonucleotide reductase (RNR) inhibition, endoplasmic reticulum stress induction, and regulation of other cancer signaling pathways. Their ability to moderately inhibit R2 RNR protein in the presence of dithiothreitol is likely related to Fe chelating properties of the proligands liberated upon reduction.

MODULATORS OF ESTROGEN RECEPTOR PROTEOLYSIS AND ASSOCIATED METHODS OF USE

The present disclosure relates to bifunctional compounds, which find utility as modulators of estrogen receptor (target protein). In particular, the present disclosure is directed to bifunctional compounds, which contain on one end a cereblon, Von Hippel-Lindau ligase-binding moiety, Inhibitors of Apotosis Proteins, or mouse double-minute homolog 2 ligand, which binds to the respective E3 ubiquitin ligase, and on the other end a moiety which binds the target protein, such that the target protein is placed in proximity to the ubiquitin ligase to effect degradation (and inhibition) of target protein. The present disclosure exhibits a broad range of pharmacological activities associated with degradation/inhibition of target protein. Diseases or disorders that result from aggregation or accumulation of the target protein are treated or prevented with compounds and compositions of the present disclosure.

A class of 2, 3 - dihydronaphth block pyrimidine analogs, its synthetic method, pharmaceutical composition and use thereof

The invention belongs to the technical field of medicines and relates to a 2,3-dihydronaphthalene-embedded m-diazabenzene analogue represented as the following general formula I and a preparation method thereof. The 2,3-dihydronaphthalene-embedded m-diazabenzene analogue has a function of inhibiting biological activities of different subtypes of a protein-tyrosine-phosphatase family (PTPases), can be used as a tool compound for researching a biological function correlation of the subtypes of the protein-tyrosine-phosphatase family (PTPases) in a cell signal transduction process, and provides a new approach for preventing and treating cancer, metabolic and immunological diseases, angiocardiopathy and neurological diseases.

INHIBITORS OF COLLAGEN PROLYL 4-HYDROXYLASE

Biheteroaryl dicarboxylates and esters, and salts thereof which are useful as modulators of CP4H activity and more particularly as inhibitors of CP4H. Compounds of formula: and salts thereof where: X is S, O, NH, or NR, where R is an alkyl group having 1-3 carbon atoms; R1 and R2 independently are —OR7, or —NHSO2R8, where R7 is selected from: hydrogen, alkyl, alkenyl, alkoxyalkyl, —R′—CO—R″, —R′—CO—O—R″, —CO—R″, —R′—O—CO—R″, —R′—CO—NR″, —CO—NR″, or —R′—O—CO—NR″, and R8 is selected from hydrogen, alkyl, aryl, arylalkyl; R3, R4 and R6 independently are hydrogen, alkyl, alkoxy, alkenyl, alkenoxy, halo alkyl, haloalkenyl, halogen, hydroxyl, hydroxyalkyl, hydroxyalkenyl, aryl, aryloxy, arylalkyl or arylalkyloxy; R5 is hydrogen, halogen, alkyl having 1-3 carbon atoms, or alkoxy having 1-3 carbon atoms; —R′— is a divalent straight chain or branched alkylene, and —R″ is an alkyl, alkenyl, arylalkyl, or aryl group. Methods for inhibition of CP4H in vivo and in vitro.

BTK INHIBITORS

The present invention provides Bruton's Tyrosine Kinase (Btk) inhibitor compounds according to Formula (I), or pharmaceutically acceptable salts or stereoisomers thereof, or to pharmaceutical compositions comprising these compounds and to their use in therapy. In particular, the present invention relates to the use of Btk inhibitor compounds of Formula (I) in the treatment of Btk mediated disorders.

1H-2,3-Dihydroperimidine derivatives: A new class of potent protein Tyrosine Phosphatase 1B inhibitors

A series of 1H-2,3-dihydroperimidine derivatives was designed, synthesized, and evaluated as a new class of inhibitors of protein tyrosine phosphatase 1B (PTP1B) with IC50 values in the micromolar range. Compounds 46 and 49 showed submicromolar inhibitory activity against PTP1B, and good selectivity (3.48-fold and 2.10-fold respectively) over T-cell protein tyrosine phosphatases (TCPTP). These results have provided novel lead compounds for the design of inhibitors of PTP1B as well as other PTPs.