39640-08-9

Basic information

• Product Name: PIPERAZIN-1-YL-PYRIDIN-3-YL-METHANONE
• Synonyms: 1-(PYRIDIN-3-YLCARBONYL)PIPERAZINE;TIMTEC-BB SBB010855;PIPERAZIN-1-YL-PYRIDIN-3-YL-METHANONE;Piperazine, 1-(3-pyridinylcarbonyl)- (9CI);1-Piperazinyl(3-pyridinyl)methanone hydrochloride;1-(3-Pyridinecarbonyl)piperazine 2HCl;1-(pyridin-3-ylcarbonyl)piperazine dihydrochloride
• CAS NO: 39640-08-9
• Molecular Formula: C₁₀H₁₃N₃O
• Molecular Weight: 191.23
• Product Categories: PIPERIDINE
• Mol File: 39640-08-9.mol
• Article Data: 9

Chemical Properties

• Boiling Point: 366.9 °C at 760 mmHg
• Flash Point: 175.7 °C
• Appearance: /
• Density: 1.167 g/cm³
• Vapor Pressure: 1.42E-05mmHg at 25°C
• Refractive Index: 1.561
• Storage Temp.: 2-8°C
• CAS DataBase Reference: PIPERAZIN-1-YL-PYRIDIN-3-YL-METHANONE(CAS DataBase Reference)
• NIST Chemistry Reference: PIPERAZIN-1-YL-PYRIDIN-3-YL-METHANONE(39640-08-9)
• EPA Substance Registry System: PIPERAZIN-1-YL-PYRIDIN-3-YL-METHANONE(39640-08-9)

Safety Data

• HazardClass: IRRITANT
• Hazardous Substances Data: 39640-08-9(Hazardous Substances Data)

Usage

General Description

PIPERAZIN-1-YL-PYRIDIN-3-YL-METHANONE is a chemical compound with a molecular formula C12H14N4O. This organic compound contains a piperazine ring and a pyridine ring, as well as a ketone functional group. It is often used as a reagent in the synthesis of other organic compounds and can also be employed in pharmaceutical research and drug development. Additionally, PIPERAZIN-1-YL-PYRIDIN-3-YL-METHANONE has potential applications as a ligand in coordination chemistry and as a building block in organic synthesis. Its properties and reactivity make it a versatile compound with multiple potential uses in various fields of chemistry and industry.

InChI:InChI=1/C10H13N3O/c14-10(9-2-1-3-12-8-9)13-6-4-11-5-7-13/h1-3,8,11H,4-7H2

Upstream product

• 110-85-0 piperazine 
• 59-67-6 nicotinic acid 
• 10400-19-8 3-pyridinecarbonyl chloride 
• 78348-28-4 nicotinic acid succinimidyl ester 
• 1071521-50-0 tert-butyl 4-((4-chlorophenyl)carbamoyl)piperazine-1-carboxylate 

Relevant articles and documents

Synthesis and evaluation of 2-(4-[4-acetylpiperazine-1-carbonyl] phenyl)-1H-benzo[d]imidazole-4-carboxamide derivatives as potential PARP-1 inhibitors and preliminary study on structure-activity relationship

Although 1H-benzo[d]imidazole-4-carboxamide derivatives have been explored for a long time, the structure–activity relationship of the substituents in the hydrophobic pocket (AD binding sites) has not thoroughly discovered. Here in, a series of 2-(4-[4-acetylpiperazine-1-carbonyl]phenyl)-1H-benzo[d]imidazole-4-carboxamide derivatives have been designed, synthesized, and successful characterization as novel and effective poly ADP-ribose polymerases (PARP)-1 inhibitors to improve the structure–activity relationships about the substituents in the hydrophobic pocket. These derivatives were evaluated for their PARP-1 inhibitory activity and cellular inhibitory against BRCA-1 deficient cells (MDA-MB-436) and wild cells (MCF-7) using PARP kit assay and MTT method. The results indicated that compared with other heterocyclic compounds, furan ring-substituted derivatives 14n-14q showed better PARP-1 inhibitory activity. Among this derivatives, compound 14p displayed the strongest inhibitory effects on PARP-1 enzyme (IC50?=?0.023 μM), which was close to that of Olaparib. 14p (IC50?=?43.56 ± 0.69 μM) and 14q (IC50?=?36.69 ± 0.83 μM) displayed good antiproliferation activity on MDA-MB-436 cells and inactivity on MCF-7 cells, indicating that 14p and 14q have high selectivity and targeting. The molecular docking method was used to explore the binding mode of compound 14p and PARP-1, and implied that the formation of hydrogen bond was essential for PARP-1 inhibition activities. This study also showed that in the hydrophobic pocket (AD binding sites), the introduction of strong electronegative groups (furan ring, e.g.) or halogen atoms in the side chain of benzimidazole might improve its inhibitory activity and this strategy could be applied in further research.

Structure-Activity Relationships of Potent, Targeted Covalent Inhibitors That Abolish Both the Transamidation and GTP Binding Activities of Human Tissue Transglutaminase

Human tissue transglutaminase (hTG2) is a multifunctional enzyme. It is primarily known for its calcium-dependent transamidation activity that leads to formation of an isopeptide bond between glutamine and lysine residues found on the surface of proteins, but it is also a GTP binding protein. Overexpression and unregulated hTG2 activity have been associated with numerous human diseases, including cancer stem cell survival and metastatic phenotype. Herein, we present a series of targeted covalent inhibitors (TCIs) based on our previously reported Cbz-Lys scaffold. From this structure-activity relationship (SAR) study, novel irreversible inhibitors were identified that block the transamidation activity of hTG2 and allosterically abolish its GTP binding ability with a high degree of selectivity and efficiency (kinact/KI > 105 M-1 min-1). One optimized inhibitor (VA4) was also shown to inhibit epidermal cancer stem cell invasion with an EC50 of 3.9 μM, representing a significant improvement over our previously reported "hit" NC9.

Synthesis and biological evaluation of substituted 4-(thiophen-2-ylmethyl)- 2H-phthalazin-1-ones as potent PARP-1 inhibitors

We have developed a series of substituted 4-(thiophen-2-ylmethyl)-2H- phthalazin-1-ones as potent PARP-1 inhibitors. Preliminary biological evaluation indicated that most compounds possessed inhibitory potencies comparable to, or higher than AZD-2281. Among these compounds, 18q appeared to be the most notable one, which displayed an 8-fold improvement in enzymatic activity compared to AZD-2281. These efforts lay the foundation for our further investigation.