108281-61-4

Basic information

• Product Name: 2-benzyl-1H-benzo[d]imidazol-5-amine
• Synonyms: 2-benzyl-1H-benzo[d]imidazol-5-amine
• CAS NO: 108281-61-4
• Molecular Weight: 223.277
• Mol File: 108281-61-4.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: 2-benzyl-1H-benzo[d]imidazol-5-amine(CAS DataBase Reference)
• NIST Chemistry Reference: 2-benzyl-1H-benzo[d]imidazol-5-amine(108281-61-4)
• EPA Substance Registry System: 2-benzyl-1H-benzo[d]imidazol-5-amine(108281-61-4)

Safety Data

• Hazardous Substances Data: 108281-61-4(Hazardous Substances Data)

Upstream product

• 7189-72-2 2-benzyl-5-nitro-1H-benzo[d]imidazole 
• 103-82-2 phenylacetic acid 
• 99-56-9 4-Nitrophenylene-1,2-diamine 
• 95-54-5 1,2-diamino-benzene 
• 621-72-7 2-benzylbenzimidazole 
• 615-47-4 benzene-1,2,4-triamine dihydrochloride 

Downstream Products

• 108281-63-6 Methyl 2-Benzylbenzimidazole-5-carbamate 
• 108281-65-8 N¹,N³-bis-(2-Benzylbenzimidazole-5-yl)urea 
• 108281-66-9 Ethyl 2-Benzylbenzimidazole-5-carbamate 
• 108318-61-2 Ethyl 2-Benzyl-1-carboethoxybenzimidazole-5-carbamate 
• 108281-64-7 Methyl 2-Benzyl-1-carbomethoxybenzimidazole-5-carbamate 
• 202272-71-7 (2-benzyl-1H-benzimidazol-5-yl)-(6-chloro-pyrido[3,4-d]pyrimidin-4-yl)-amine 
• 845658-32-4 2-benzyl-N-(5-iodopyrimidin-4-yl)-1H-benzimidazol-5-amine 

Relevant articles and documents

Targeting Her2-insYVMA with Covalent Inhibitors - A Focused Compound Screening and Structure-Based Design Approach

Mutated or amplified Her2 serves as a driver of non-small cell lung cancer or mediates resistance toward the inhibition of its family member epidermal growth factor receptor with small-molecule inhibitors. To date, small-molecule inhibitors targeting Her2 which can be used in clinical routine are lacking, and therefore, the development of novel inhibitors was undertaken. In this study, the well-established pyrrolopyrimidine scaffold was modified with structural motifs identified from a screening campaign with more than 1600 compounds, which were applied against wild-type Her2 and its mutant variant Her2-A775_G776insYVMA. The resulting inhibitors were designed to covalently target a reactive cysteine in the binding site of Her2 and were further optimized by means of structure-based drug design utilizing a set of obtained complex crystal structures. In addition, the analysis of binding kinetics and absorption, distribution, metabolism, and excretion parameters as well as mass spectrometry experiments and western blot analysis substantiated our approach.