127404-21-1

Basic information

• Product Name: Benzaldehyde, 4-(4-methyl-1H-imidazol-1-yl)-
• Synonyms: Benzaldehyde, 4-(4-methyl-1H-imidazol-1-yl)-;4-(4-Methyl-1H-iMidazol-1-yl)-;4-(4-methylimidazol-1-yl)benzaldehyde
• CAS NO: 127404-21-1
• Molecular Formula: C₁₁H₁₀N₂O
• Molecular Weight: 186.2099
• Mol File: 127404-21-1.mol
• Article Data: 7

Chemical Properties

• Boiling Point: 364.6°C at 760 mmHg
• Flash Point: 174.3°C
• Appearance: /
• Density: 1.13g/cm³
• Vapor Pressure: 1.67E-05mmHg at 25°C
• Refractive Index: 1.593
• CAS DataBase Reference: Benzaldehyde, 4-(4-methyl-1H-imidazol-1-yl)-(CAS DataBase Reference)
• NIST Chemistry Reference: Benzaldehyde, 4-(4-methyl-1H-imidazol-1-yl)-(127404-21-1)
• EPA Substance Registry System: Benzaldehyde, 4-(4-methyl-1H-imidazol-1-yl)-(127404-21-1)

Safety Data

• Hazardous Substances Data: 127404-21-1(Hazardous Substances Data)

Usage

General Description

Benzaldehyde, 4-(4-methyl-1H-imidazol-1-yl)-, also known as 4-(4-methylimidazol-1-yl)benzaldehyde, is a chemical compound with the molecular formula C10H10N2O. It is a derivative of benzaldehyde and contains a methyl group and an imidazole ring. Benzaldehyde, 4-(4-methyl-1H-imidazol-1-yl)- is commonly used in organic synthesis and pharmaceutical research, particularly in the development of anti-inflammatory and antifungal medications. It has also been studied for its potential role in the treatment of neurodegenerative diseases. Benzaldehyde, 4-(4-methyl-1H-imidazol-1-yl)- is a versatile building block for the synthesis of various biologically active compounds, making it an important compound in medicinal chemistry and drug development.

InChI:InChI=1/C11H10N2O/c1-9-6-13(8-12-9)11-4-2-10(7-14)3-5-11/h2-8H,1H3

Upstream product

• 822-36-6 4-methyl-1H-imidazole 
• 459-57-4 4-fluorobenzaldehyde 

Downstream Products

• 1160360-11-1 C₂₇H₂₇ClFN₃O₃S 
• 1160360-08-6 C₂₅H₂₆F₃N₃O₄ 
• 1128103-39-8 C₂₅H₂₄FN₃O₃ 
• 1160359-88-5 1-[1-(4-fluorophenyl)ethyl]-3-{hydroxy[3-methoxy-4-(4-methylimidazol-1-yl)phenyl]methyl}piperidin-2-one 
• 167758-77-2 (4-(4-methyl-1H-imidazol-1-yl)phenyl)methanol 
• 1093980-62-1 1-(4-ethynylphenyl)-4-methyl-1H-imidazole 
• 1614229-03-6 N-(3-cyclopropyl-1-phenyl-1H-pyrazol-5-yl)-2-(4-(4-(4-methyl-1H-imidazole-1-yl)phenyl)-1H-1,2,3-triazol-1-yl)acetamide 

Relevant articles and documents

Reversible Covalent Imine-Tethering for Selective Stabilization of 14-3-3 Hub Protein Interactions

The stabilization of protein complexes has emerged as a promising modality, expanding the number of entry points for novel therapeutic intervention. Targeting proteins that mediate protein-protein interactions (PPIs), such as hub proteins, is equally challenging and rewarding as they offer an intervention platform for a variety of diseases, due to their large interactome. 14-3-3 hub proteins bind phosphorylated motifs of their interaction partners in a conserved binding channel. The 14-3-3 PPI interface is consequently only diversified by its different interaction partners. Therefore, it is essential to consider, additionally to the potency, also the selectivity of stabilizer molecules. Targeting a lysine residue at the interface of the composite 14-3-3 complex, which can be targeted explicitly via aldimine-forming fragments, we studied the de novo design of PPI stabilizers under consideration of potential selectivity. By applying cooperativity analysis of ternary complex formation, we developed a reversible covalent molecular glue for the 14-3-3/Pin1 interaction. This small fragment led to a more than 250-fold stabilization of the 14-3-3/Pin1 interaction by selective interfacing with a unique tryptophan in Pin1. This study illustrates how cooperative complex formation drives selective PPI stabilization. Further, it highlights how specific interactions within a hub proteins interactome can be stabilized over other interactions with a common binding motif.

Discovery and Optimization of a Novel Triazole Series of GPR142 Agonists for the Treatment of Type 2 Diabetes

GPR142 has been identified as a potential glucose-stimulated insulin secretion (GSIS) target for the treatment of type 2 diabetes mellitus (T2DM). A class of triazole GPR142 agonists was discovered through a high throughput screen. The lead compound 4 suffered from poor metabolic stability and poor solubility. Lead optimization strategies to improve potency, efficacy, metabolic stability, and solubility are described. This optimization led to compound 20e, which showed significant reduction of glucose excursion in wild-type but not in GPR142 deficient mice in an oral glucose tolerance test (oGTT) study. These studies provide strong evidence that reduction of glucose excursion through treatment with 20e is GPR142-mediated, and GPR142 agonists could be used as a potential treatment for type 2 diabetes.

Maximizing diversity from a kinase screen: Identification of novel and selective pan-Trk inhibitors for chronic pain

We have identified several series of small molecule inhibitors of TrkA with unique binding modes. The starting leads were chosen to maximize the structural and binding mode diversity derived from a high throughput screen of our internal compound collection. These leads were optimized for potency and selectivity employing a structure based drug design approach adhering to the principles of ligand efficiency to maximize binding affinity without overly relying on lipophilic interactions. This endeavor resulted in the identification of several small molecule pan-Trk inhibitor series that exhibit high selectivity for TrkA/B/C versus a diverse panel of kinases. We have also demonstrated efficacy in both inflammatory and neuropathic pain models upon oral dosing. Herein we describe the identification process, hit-to-lead progression, and binding profiles of these selective pan-Trk kinase inhibitors.