57018-46-9

Basic information

• Product Name: 4-AZIDOPHENACYL BROMIDE
• Synonyms: 4-Azidophenacyl bromide powder;P-AZIDOPHENACYL BROMIDE;4-AZIDOPHENACYL BROMIDE;1-(4-azidophenyl)-2-bromoethan-1-one;4'-Azido-2-bromoacetophenone;1-(4-Azidophenyl)-2-bromo-ethanone;4μ-Azido-2-bromoacetophenone, 4-Azido-α-bromoacetophenone;4'-Azido-α-bromoacetophenone
• CAS NO: 57018-46-9
• Molecular Formula: C₈H₆BrN₃O
• Molecular Weight: 240.06
• EINECS: 260-519-5
• Product Categories: Affinity Chromatography;Photoaffinity Labels;Aromatics;MTS & Sulfhydryl Active Reagents;Sulfur & Selenium Compounds
• Mol File: 57018-46-9.mol

Chemical Properties

• Melting Point: 64-65 °C
• Appearance: yellow/powder
• Storage Temp.: 2-8°C
• Solubility: methanol: 50 mg/mL
• BRN: 1961705
• CAS DataBase Reference: 4-AZIDOPHENACYL BROMIDE(CAS DataBase Reference)
• NIST Chemistry Reference: 4-AZIDOPHENACYL BROMIDE(57018-46-9)
• EPA Substance Registry System: 4-AZIDOPHENACYL BROMIDE(57018-46-9)

Safety Data

• Hazard Codes: F,C
• Statements: 11-34-42/43
• Safety Statements: 16-26-27-36/37/39-45
• RIDADR: UN 1325 4.1/PG 2
• WGK Germany: 3
• F: 4.5-8-10-19
• HazardClass: 4.1
• PackingGroup: III
• Hazardous Substances Data: 57018-46-9(Hazardous Substances Data)

Usage

Uses

Used in Enzyme Research:
4-AZIDOPHENACYL BROMIDE is used as a research tool in the enzyme industry for investigating the active sites of sulfhydryl enzymes. Its ability to couple with reactive cysteine residues at the active site allows scientists to gain insights into enzyme function and mechanism.
Used in Photocross-linking Applications:
In the field of photocross-linking, 4-AZIDOPHENACYL BROMIDE is used as a heterobifunctional cross-linking reagent. It typically couples to sulfhydryl groups in the pH range of 7.0-8.0, and upon UV irradiation at 250 nm, it forms a reactive nitrene that leads to rapid and non-specific bonding. This property makes it valuable for studying protein-protein interactions and other molecular interactions.
Used in Ribosomal Binding Site Studies:
In the molecular biology industry, 4-AZIDOPHENACYL BROMIDE is used as a research tool for studying the nature of the ribosomal binding site of E. coli tRNAVal. Its photolabile properties enable researchers to investigate the binding mechanisms and interactions involved in protein synthesis.

InChI:InChI=1/C8H6BrN3O/c9-5-8(13)6-1-3-7(4-2-6)11-12-10/h1-4H,5H2

Upstream product

• 20062-24-2 4-azidoacetophenone 
• 186581-53-3 diazomethane 
• 14848-01-2 4-azidobenzoyl chloride 
• 6427-66-3 4-azidobenzoic acid 
• 99-92-3 p-aminobenzophenone 

Downstream Products

• 1190333-55-1 2-amino-5-(4-azidophenyl)imidazole-1-carboxylic acid tert-butyl ester 
• 1190333-83-5 5-(4-azidophenyl)-2-tert-butoxycarbonylaminoimidazole-1-carboxylic acid tert-butyl ester 
• 1190333-59-5 2-amino-5-(4-heptanoylaminophenyl)imidazole-1-carboxylic acid tert-butyl ester 
• 1190333-56-2 5-(4-azidophenyl)-2-(di-tert-butoxycarbonylamino)imidazole-1-carboxylic acid tert-butyl ester 
• 1190333-21-1 heptanoic acid [4-(2-amino-3H-imidazol-4-yl)phenyl]amide hydrochloride 
• 1190333-13-1 [4-(2-amino-3H-imidazol-4-yl)phenyl]-3,5-difluorobenzamide hydrochloride 
• 1190333-84-6 2-tert-butoxycarbonylamino-5-{4-[4-(4-pentylphenyl)-[1,2,3]triazol-1-yl]phenyl}imidazole-1-carboxylic acid tert-butyl ester 
• 1190333-57-3 2-(di-tert-butoxycarbonylamino)-5-[4-(3,5-difluorobenzoylamino)phenyl]imidazole-1-carboxylic acid tert-butyl ester 
• 73322-71-1 S-(4-azidophenacyl)glutathione 
• 65321-87-1 4-(4-azido-phenyl)-thiazol-2-ylamine 

Relevant articles and documents

Small Molecule Control of Morpholino Antisense Oligonucleotide Function through Staudinger Reduction

Conditionally activated, caged morpholino antisense agents (cMOs) are tools that enable the temporal and spatial investigation of gene expression, regulation, and function during embryonic development. Cyclic MOs are conformationally gated oligonucleotide analogs that do not block gene expression until they are linearized through the application of an external trigger, such as light or enzyme activity. Here, we describe the first examples of small molecule-responsive cMOs, which undergo rapid and efficient decaging via a Staudinger reduction. This is enabled by a highly flexible linker design that offers opportunities for the installation of chemically activated, self-immolative motifs. We synthesized cyclic cMOs against two distinct, developmentally relevant genes and demonstrated phosphine-triggered knockdown of gene expression in zebrafish embryos. This represents the first report of a small molecule-triggered antisense agent for gene knockdown, adding another bioorthogonal entry to the growing arsenal of gene knockdown tools.

Identification of Anti-Mycobacterial Biofilm Agents Based on the 2-Aminoimidazole Scaffold

Tuberculosis (TB) remains a significant global health problem for which new therapeutic options are sorely needed. The ability of the causative agent, Mycobacterium tuberculosis, to reside within host macrophages and form biofilm-like communities contributes to the persistent and drug-tolerant nature of the disease. Compounds that can prevent or reverse the biofilm-like phenotype have the potential to serve alongside TB antibiotics to overcome this tolerance, and decrease treatment duration. Using Mycobacterium smegmatis as a surrogate organism, we report the identification of two new 2-aminoimidazole compounds that inhibit and disperse mycobacterial biofilms, work synergistically with isoniazid and rifampicin to eradicate preformed M. smegmatis biofilms in vitro, are nontoxic toward Galleria mellonella, and exhibit stability in mouse plasma.

Synthesis and evaluation of non-dimeric HCV NS5A inhibitors

Based on the symmetrical bidentate structure of the NS5A inhibitor BMS-790052, a series of new monodentate molecules were designed. The synthesis of 36 new non-dimeric NS5A inhibitors is reported along with their ability to block HCV replication in an HCV 1b replicon system. Among them compound 5a showed picomolar range activity along with an excellent selectivity index (SI > 90,000).

Identification of aryl 2-aminoimidazoles as biofilm inhibitors in Gram-negative bacteria

The synthesis and biofilm inhibitory activity of a 30-member aryl amide 2-aminoimidazole library against the three biofilm forming Gram-negative bacteria Escherichia coli, Psuedomonas aeruginosa, and Acinetobacter baumannii is presented. The most active compound identified inhibits the formation of E. coli biofilms with an IC50 of 5.2 μM and was observed to be non-toxic to planktonic growth, demonstrating that analogues based on an aryl framework are viable options as biofilm inhibitors within the 2-aminoimidazole family.

INHIBITION OF BACTERIAL BIOFILMS WITH IMIDAZOLE-PHENYL DERIVATIVES

Disclosure is provided for imidazole-phenyl derivative compounds that prevent, remove and/or inhibit the formation of biofilms, compositions comprising these compounds, devices comprising these compounds, and methods of using the same.

Template-competitive inhibitors of HIV-1 reverse transcriptase: design, synthesis and inhibitory activity.

We report the design, synthesis and activity studies on a novel class of template-competitive reverse transcriptase inhibitors (TCRTIs). The TCRTIs are 1,N(6)-etheno analogues of a series of dATP-based template-competitive DNA polymerase inhibitors synthesized in our laboratory (Moore, B. M.; Jalluri, R.; Doughty, M.B. Biochemistry 1996, 35, 11634). Thus, nucleotides 2-(4-azidophenacyl)thio-1,N(6)-etheno-2'-deoxyadenosine 5'-triphosphate 1, the tetrafluoro analogue 2-(4-azido-2,3,5,6-tetrafluorophenacyl)thio-1,N(6)-etheno-2'-deoxyadenosine 5'-triphosphate 2 and its analogues were synthesized by alkylation of 2-thio-1,N(6)-etheno-2'-deoxyadenosine 5'-monophosphate with the corresponding chloro- or bromo-alkyl halides and converted to the triphosphate. Kinetically, nucleotides 1 and 2 are both competitive inhibitors of reverse transcriptase versus template/primer with K(i)'s of 8.0 and 7.4 microM, respectively, and non-competitive inhibitors versus TTP with K(i)'s of 15 and 10 microM, respectively. Nucleotide 3, which differs from 1 only in that it lacks the etheno group, non-complementary nucleotide triphosphates, and related monophosphates and nucleosides, are completely inactive as inhibitors of reverse transcriptase at concentrations up to 1 mM. Photoinactivation of RT by 1 was both time- and concentration-dependent, and protected by template/primer but not by dNTPs. The concentration-dependent inactivation data gave a K(D,app) of 17.2 microM and maximum inactivation of 90%, and radiolabeled [beta, gamma-32P]-1 photoincorporated specifically and covalently into the p66 subunit of RT. Thus the photoinactivation data support our main conclusion from the kinetic data that this class of RT inhibitors are non-substrate and template-competitive.

Design and synthesis of celecoxib and rofecoxib analogues as selective cyclooxygenase-2 (COX-2) inhibitors: Replacement of sulfonamide and methylsulfonyl pharmacophores by an azido bioisostere

Celecoxib (13) and rofecoxib (17) analogues, in which the respective SO2NH2 and SQ2Me hydrogen-bonding pharmacophores were replaced by a dipolar azido bioisosteric substituent, were investigated. Molecular modeling (docking) studies showed that the azido substituent of these two analogues (13, 17) was inserted deep into the secondary pocket of the human COX-2 binding site where it undergoes electrostatic interaction with Arg513. The azido analogue of rofecoxib (17), the most potent and selective inhibitor of COX-2 (COX-1 IC50 = 159.7 μM; COX-2 IC50 = 0.196 μM; COX-2 selectivity index = 812), exhibited good oral antiinflammatory and analgesic activities.