90514-72-0

Usage

Uses

Used in Organic Synthesis:
4-(1H-1,3-BENZIMIDAZOL-1-YL)BENZENECARBALDEHYDE is used as a building block in organic synthesis for its ability to form a variety of complex organic molecules. Its unique structure allows for the creation of new compounds with potential applications in various industries.
Used in Medicinal Chemistry:
In the field of medicinal chemistry, 4-(1H-1,3-BENZIMIDAZOL-1-YL)BENZENECARBALDEHYDE is used as a key component in the development of pharmaceutical drugs. Its presence in the molecular structure of certain drugs suggests that it may contribute to their therapeutic effects, making it a valuable asset in drug design and synthesis.
Used in Pharmaceutical Drug Development:
4-(1H-1,3-BENZIMIDAZOL-1-YL)BENZENECARBALDEHYDE is being researched for its potential therapeutic applications, particularly in the development of new pharmaceutical drugs. Its incorporation into drug molecules may enhance their efficacy, selectivity, and safety, leading to improved treatments for various medical conditions.
Used in Research and Development:
4-(1H-1,3-BENZIMIDAZOL-1-YL)BENZENECARBALDEHYDE is also utilized in research and development settings to explore its pharmacological properties and potential biological activities. Understanding its interactions with biological systems can provide insights into the development of novel therapeutic agents and contribute to advancements in medicine.

Upstream product

• 51-17-2 benzoimidazole 
• 459-57-4 4-fluorobenzaldehyde 
• 104-88-1 4-chlorobenzaldehyde 
• 1122-91-4 4-bromo-benzaldehyde 
• 87199-17-5 4-formylphenylboronic acid, 

Downstream Products

• 117607-04-2 6-[(E)-2-(4-Benzoimidazol-1-yl-phenyl)-vinyl]-5-methyl-4,5-dihydro-2H-pyridazin-3-one 
• 220495-52-3 4-(benzimidazole-1-yl)benzoic acid 
• 1392592-93-6 4-(4-(1H-benzo[d]imidazol-1-yl) phenyl)-6-(4-methoxyphenyl)pyrimidin-2-amine 
• 1392592-90-3 4-(4-(1H-benzo[d]imidazol-1-yl)phenyl)-6-(4-chlorophenyl)pyrimidin-2-amine 
• 1392592-92-5 4-(4-(1H-benzo[d]imidazol-1-yl) phenyl)-6-(4-bromophenyl)pyrimidin-2-amine 
• 1392592-89-0 4-(4-(1H-benzo[d]imidazol-1-yl)phenyl)-6-(4 fluorophenyl)pyrimidin-2-amine 
• 1392592-91-4 4-(4-(1H-benzo[d]imidazol-1-yl)phenyl)-6-(2,4-dichlorophenyl)pyrimidin-2-amine 
• 666850-93-7 (4aS,8aR)-2-[1-(4-benzimidazol-1-yl-benzyl)-piperidin-4-yl]-4-(3,4-dimethoxy-phenyl)-4a,5,8,8a-tetrahydro-2H-phthalazin-1-one hydrochloride 
• 90514-84-4 5-(4-Benzoimidazol-1-yl-phenyl)-6-methyl-2-oxo-1,2-dihydro-pyridine-3-carbonitrile 
• 108122-61-8 1-(4-Benzoimidazol-1-yl-phenyl)-propan-2-one 
• 90514-75-3 1-[4-((E)-2-Nitro-propenyl)-phenyl]-1H-benzoimidazole 

Relevant academic research and scientific papers

Synthesis and antimicrobial activity of novel 2-[4-(1H-benzimidazol-1-yl) phenyl]-1H-benzimidazoles

A new class of 2-[4-(1H-benzimidazol-1-yl)phenyl]-1H-benzimidazoles (13-22) were synthesized via cyclocondensation reaction of the substituted 1,2-phenylenediamines (1, 4-12) and 1-(4-formylpheny)-1H-benzimidazole (3). The synthesized compounds were evalu

Synthesis and anticandidal activity evaluation of new benzimidazole-thiazole derivatives

Azole-based antifungal agents constitute one of the important classes of antifungal drugs. Hence, in the present work, 12 new benzimidazole-thiazole derivatives 3a-3l were synthesized to evaluate their anticandidal activity against C. albicans, C. glabrata, C. krusei, and C. parapsilopsis. The structures of the newly synthesized compounds 3a-3l were confirmed by IR, H-NMR, C-NMR, and ESI-MS spectroscopic methods. ADME parameters of synthesized compounds 3a-3l were predicted by an in-slico study and it was determined that all synthesized compounds may have a good pharmacokinetic profile. In the anticandidal activity studies, compounds 3c and 3d were found to be the most active compounds against all Candida species. In addition, cytoxicity studies showed that these compounds are nontoxic with a IC50 value higher than 500 μg/mL. The effect of compounds 3c and 3d on the ergosterol level of C. albicans was determined by an LC-MS-MS method. It was observed that both compounds cause a decrease in the ergosterol level. A molecular docking study including binding modes of 3c to lanosterol 14α-demethylase (CYP51), a key enzyme in ergosterol biosynthesis, was performed to elucidate the mechanism of the antifungal action. The docking studies revealed that there is a strong interaction between CYP51 and the most active compound 3c.

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.

Benzimidazole benzaldehyde fluorescein hydrazide Schiff base and preparation method thereof

The invention belongs to the field of fluorescent probes, and particularly relates to benzimidazole benzaldehyde fluorescein hydrazide Schiff base and a preparation method thereof. The probe is a turn-on type fluorescent probe, the probe utilizes a photoi

Benzimidazolyl benzaldehyde condensed rhodamine hydrazine hydrate Schiff base and preparation method thereof

The invention belongs to the field of fluorescent probes, and particularly relates to a benzimidazolyl benzaldehyde rhodamine hydrazine hydrate Schiff base fluorescent probe. A fluorescent switch is turned on in the presence of iron ions by utilizing a ph

PROTEIN-PROTEIN INTERACTION STABILIZERS

Provided herein, inter alia, are stabilizers of protein-protein interactions and methods of identifying and using the same.

Cu(OAc)2-porphyrins as an efficient catalytic system for base-free, nature mimicking Chan–Lam coupling in water

The use of porphyrins as ligands in organic synthesis reveals the natural process, because these are the constituent motifs of catalysts in many bio-organic reactions. This article presents the synthesis of two N-pincer tetradentate porphyrins; tetrasodium meso-tetra(p-sulfonatophenyl)phorphyrin (H2TSTpSPP) and meso-tetra(m-carboxyphenyl)porphyrin (H2TmCPP), and study on their aptness for Cu-catalyzed C–N coupling reactions of arylboronic acids and amines (Chan–Lam coupling reaction) in water under external base free conditions. The porphyrins and Chan–Lam coupling products were well characterized by their spectral analysis. The high product yields, application of nature-inspired conditions, large extent of substrates, ease of making and handling the ligands, avoidance of base, and use of water as reaction media are the attractive attributes of this finding.

Design, Synthesis, and Biological Evaluation of Novel Allosteric Protein Disulfide Isomerase Inhibitors

Protein disulfide isomerase (PDI) is responsible for nascent protein folding in the endoplasmic reticulum (ER) and is critical for glioblastoma survival. To improve the potency of lead PDI inhibitor BAP2 ((E)-3-(3-(4-hydroxyphenyl)-3-oxoprop-1-en-1-yl)benzonitrile), we designed and synthesized 67 analogues. We determined that PDI inhibition relied on the A ring hydroxyl group of the chalcone scaffold and cLogP increase in the sulfonamide chain improved potency. Docking studies revealed that BAP2 and analogues bind to His256 in the b′ domain of PDI, and mutation of His256 to Ala abolishes BAP2 analogue activity. BAP2 and optimized analogue 59 have modest thiol reactivity; however, we propose that PDI inhibition by BAP2 analogues depends on the b′ domain. Importantly, analogues inhibit glioblastoma cell growth, induce ER stress, increase expression of G2M checkpoint proteins, and reduce expression of DNA repair proteins. Cumulatively, our results support inhibition of PDI as a novel strategy to treat glioblastoma.

Design and Synthesis of 2-Substitutedphenyl Benzo[D]Thiazole Derivatives and Their β-Amyloid Aggregation and Cholinesterase Inhibitory Activities

The occurrence of amyloid-β (Aβ) and reduced cholinergic tranmission are two major hallmarks of Alzheimer’s disease (AD). Therefore, a series of new 2-phenylbenzo[d]thiazoles substituted with azole/piperazine moieties were designed, synthesized, and evaluated as potential dual inhibitors of Aβ aggregation and cholinesterase (ChE) activities. In vitro studies showed that compound 2m containing an imidazole ring strongly inhibited Aβ1–40 (49.2%) and Aβ1-42 aggregation (60.6%). All derivatives exhibited weak inhibitory activities against both acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). Therefore, compound 2m may represent promising therapeutic option for inhibiting Aβ-mediated pathology in AD.

Novel 2-Arylbenzimidazole derivatives as multi-targeting agents to treat Alzheimer’s disease

This study describes the synthesis, pharmacological evaluation, including acetylcholinesterase (AChE)/butyrylcholinesterase (BChE) inhibition, amyloid beta (Aβ) antiaggregation, and neuroprotective effects, as well as molecular modeling of novel 2-(4-subs