126963-65-3

Basic information

• Product Name: N-benzyl-5-bromopentanamide
• Synonyms: N-benzyl-5-bromopentanamide
• CAS NO: 126963-65-3
• Molecular Weight: 270.169
• Mol File: 126963-65-3.mol

Chemical Properties

• CAS DataBase Reference: N-benzyl-5-bromopentanamide(CAS DataBase Reference)
• NIST Chemistry Reference: N-benzyl-5-bromopentanamide(126963-65-3)
• EPA Substance Registry System: N-benzyl-5-bromopentanamide(126963-65-3)

Safety Data

• Hazardous Substances Data: 126963-65-3(Hazardous Substances Data)

Upstream product

• 4509-90-4 5-bromovaleroyl chloride 
• 100-46-9 benzylamine 
• 2067-33-6 5-bromopentanoic acid 

Downstream Products

• 126963-72-2 Benzyl-[tetrahydro-pyran-(2Z)-ylidene]-amine 
• 1026009-31-3 5-(4,5-Diphenyl-1H-imidazol-2-ylsulfanyl)-pentanoic acid benzylamide 
• 1245570-92-6 C₁₂H₁₆N₄O 
• 1244550-78-4 C₂₉H₂₆N₄O₅ 
• 161669-72-3 4,5-diphenyl-2-<<5-(benzylamino)pentyl>thio>-1H-imidazole 

Relevant articles and documents

Galantamine derivatives as acetylcholinesterase inhibitors: Docking, design, synthesis, and inhibitory activity

Galantamine (GAL) is a well-known acetylcholinesterase (AChE) inhibitor, and it is widely used for treatment of Alzheimer’s disease. GAL fits well in the catalytic site of AChE, but it is too short to block the peripheral anionic site (PAS) of the enzyme,

Novel Multitarget-Directed Ligands Aiming at Symptoms and Causes of Alzheimer's Disease

Alzheimer's disease (AD) is a major public health problem, which is due to its increasing prevalence and lack of effective therapy or diagnostics. The complexity of the AD pathomechanism requires complex treatment, e.g. multifunctional ligands targeting both the causes and symptoms of the disease. Here, we present new multitarget-directed ligands combining pharmacophore fragments that provide a blockade of serotonin 5-HT6 receptors, acetyl/butyrylcholinesterase inhibition, and amyloid β antiaggregation activity. Compound 12 has displayed balanced activity as an antagonist of 5-HT6 receptors (Ki = 18 nM) and noncompetitive inhibitor of cholinesterases (IC50hAChE = 14 nM, IC50eqBuChE = 22 nM). In further in vitro studies, compound 12 has shown amyloid β antiaggregation activity (IC50 = 1.27 μM) and ability to permeate through the blood-brain barrier. The presented findings may provide an excellent starting point for further studies and facilitate efforts to develop new effective anti-AD therapy.

Docking-based Design of Galantamine Derivatives with Dual-site Binding to Acetylcholinesterase

The enzyme acetylcholinesterase is a key target in the treatment of Alzheimer's disease because of its ability to hydrolyze acetylcholine via the catalytic binding site and to accelerate the aggregation of amyloid-β peptide via the peripheral anionic site (PAS). Using docking-based predictions, in the present study we design 20 novel galantamine derivatives with alkylamide spacers of different length ending with aromatic fragments. The galantamine moiety blocks the catalytic site, while the terminal aromatic fragments bind in PAS. The best predicted compounds are synthesized and tested for acetylcholinesterase inhibitory activity. The experimental results confirm the predictions and show that the heptylamide spacer is of optimal length to bridge the galantamine moiety bound in the catalytic site and the aromatic fragments interacting with PAS. Among the tested terminal aromatic fragments, the phenethyl substituent is the most suitable for binding in PAS.

Salicylic acid based small molecule inhibitor for the oncogenic src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2)

The Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2) plays a pivotal role in growth factor and cytokine signaling. Gain-of-function SHP2 mutations are associated with Noonan syndrome, various kinds of leukemias, and solid tumors. Thus, there is considerable interest in SHP2 as a potential target for anticancer and antileukemia therapy. We report a salicylic acid based combinatorial library approach aimed at binding both active site and unique nearby subpockets for enhanced affinity and selectivity. Screening of the library led to the identification of a SHP2 inhibitor II-B08 (compound 9) with highly efficacious cellular activity. Compound 9 blocks growth factor stimulated ERK1/2 activation and hematopoietic progenitor proliferation, providing supporting evidence that chemical inhibition of SHP2 may be therapeutically useful for anticancer and antileukemia treatment. X-ray crystallographic analysis of the structure of SHP2 in complex with 9 reveals molecular determinants that can be exploited for the acquisition of more potent and selective SHP2 inhibitors.

Targeting mycobacterium protein tyrosine phosphatase B for antituberculosis agents

Protein tyrosine phosphatases are often exploited and subverted by pathogenic bacteria to cause human diseases. The tyrosine phosphatase mPTPB from Mycobacterium tuberculosis is an essential virulence factor that is secreted by the bacterium into the cytoplasm of macrophages, where it mediates mycobacterial survival in the host. Consequently, there is considerable interest in understanding the mechanism by which mPTPB evades the host immune responses, and in developing potent and selective mPTPB inhibitors as unique antituberculosis (antiTB) agents. We uncovered that mPTPB subverts the innate immune responses by blocking the ERK1/2 and p38 mediated IL-6 production and promoting host cell survival by activating the Akt pathway. We identified a potent and selective mPTPB inhibitor I-A09 with highly efficacious cellular activity, from a combinatorial library of bidentate benzofuran salicylic acid derivatives assembled by click chemistry. We demonstrated that inhibition of mPTPB with I-A09 in macrophages reverses the altered host immune responses induced by the bacterial phosphatase and prevents TB growth in host cells. The results provide the necessary proof-of-principle data to support the notion that specific inhibitors of the mPTPB may serve as effective antiTB therapeutics.

Derivatives of salicylic acid as inhibitors of YopH in yersinia pestis

Yersinia pestis causes diseases ranging from gastrointestinal syndromes to bubonic plague and could be misused as a biological weapon. As its protein tyrosine phosphatase YopH has already been demonstrated as a potential drug target, we have developed two series of forty salicylic acid derivatives and found sixteen to have micromolar inhibitory activity. We designed these ligands to have two chemical moieties connected by a flexible hydrocarbon linker to target two pockets in the active site of the protein to achieve binding affinity and selectivity. One moiety possessed the salicylic acid core intending to target the phosphotyrosine-binding pocket. The other moiety contained different chemical fragments meant to target a nearby secondary pocket. The two series of compounds differed by having hydrocarbon linkers with different lengths. Before experimental co-crystal structures are available, we have performed molecular docking to predict how these compounds might bind to the protein and to generate structural models for performing binding affinity calculation to aid future optimization of these series of compounds.

Facile preparation of 2-imino tetrahydrofurans, pyrans and oxepans

A simple and convenient route to 2-imino tetrahydrofurans, pyrans and oxepans which utilizes a silver-assisted intramolecular O-alkylation has been developed and produces these novel imidates in good yields and with high stereoselectivity.