5181-36-2

Usage

Uses

Used in Organic Synthesis:
2-(3-bromopropoxy)-1H-isoindole-1,3(2H)-dione is used as a building block for the synthesis of novel organic molecules. Its unique structure allows for the creation of new compounds with potential applications in various fields.
Used in Pharmaceutical Research:
In the pharmaceutical industry, 2-(3-bromopropoxy)-1H-isoindole-1,3(2H)-dione is used as a potential pharmacophore for drug development. Its distinct chemical properties may contribute to the discovery of new therapeutic agents.
Further research and studies are necessary to fully explore the range of potential applications for 2-(3-bromopropoxy)-1H-isoindole-1,3(2H)-dione and to understand its capabilities in these fields.

Upstream product

• 524-38-9 N-hydroxyphthalimide 
• 627-18-9 1-bromo-3-propanol 
• 85-44-9 phthalic anhydride 
• 109-64-8 1,3-dibromo-propane 

Downstream Products

• 118856-48-7 N-[3-[4-(2-methylphenyl)-1-piperazinyl]propyloxy]phthalimide 
• 118856-28-3 N-[3-[4-(2-methoxyphenyl)-1-piperazinyl]propyloxy]phthalimide 
• 118856-29-4 N-[3-[4-(3-methylthiophenyl)-1-piperazinyl]propyloxy]phthalimide 
• 118856-47-6 N-[3-[4-(3-chlorophenyl)-1-piperazinyl]propyloxy]phthalimide 
• 847021-14-1 2-(3-{4-Oxo-2-[(E)-phenylimino]-5-[1-phenyl-meth-(Z)-ylidene]-thiazolidin-3-yl}-propoxy)-isoindole-1,3-dione 
• 847021-00-5 2-(3-{2-[(E)-4-Chloro-phenylimino]-4-oxo-thiazolidin-3-yl}-propoxy)-isoindole-1,3-dione 
• 847021-01-6 2-(3-{2-[(E)-4-Nitro-phenylimino]-4-oxo-thiazolidin-3-yl}-propoxy)-isoindole-1,3-dione 
• 847021-15-2 2-(3-{2-[(E)-4-Chloro-phenylimino]-4-oxo-5-[1-phenyl-meth-(Z)-ylidene]-thiazolidin-3-yl}-propoxy)-isoindole-1,3-dione 
• 847021-16-3 2-(3-{2-[(E)-4-Nitro-phenylimino]-4-oxo-5-[1-phenyl-meth-(Z)-ylidene]-thiazolidin-3-yl}-propoxy)-isoindole-1,3-dione 
• 847021-21-0 2-(3-{2-[(E)-4-Chloro-phenylimino]-5-[1-(4-methoxy-phenyl)-meth-(Z)-ylidene]-4-oxo-thiazolidin-3-yl}-propoxy)-isoindole-1,3-dione 
• 847021-18-5 2-(3-{2-[(E)-4-Chloro-phenylimino]-5-[1-(4-hydroxy-phenyl)-meth-(Z)-ylidene]-4-oxo-thiazolidin-3-yl}-propoxy)-isoindole-1,3-dione 
• 847021-22-1 2-(3-{5-[1-(4-Methoxy-phenyl)-meth-(Z)-ylidene]-2-[(E)-4-nitro-phenylimino]-4-oxo-thiazolidin-3-yl}-propoxy)-isoindole-1,3-dione 
• 847021-19-6 2-(3-{5-[1-(4-Hydroxy-phenyl)-meth-(Z)-ylidene]-2-[(E)-4-nitro-phenylimino]-4-oxo-thiazolidin-3-yl}-propoxy)-isoindole-1,3-dione 

Relevant academic research and scientific papers

15N-D-labeled ionic probes for mass spectrometry

An effective 15N- and deuterium (D)-labeled 2,6-bis(oxazolin-2- yl)pyridine (pybox)-La complex based probe ionization method that produces a distinct isotopic shift was developed. The distinct isotopic shift was detected by using the newly synthesized 15N-D-labeled pybox complexes. Moreover, O-[3-(tetramethylpybox)-propyl]-hydroxylamine (oxime-TMpybox) was prepared for attachment to the carbonyl group of the target molecule. Distinct isotopic shifts and multiple charged ions were detected for various compounds having amino, thiol, carboxyl, and carbonyl groups and fullerenes, using the TMpybox ionic probe series in cold-spray ionization mass spectrometry.

Post-functionalization of platinum-NHC complexes by oxime ligation for ligand targeted therapy

Carbonyl condensation reactions such as imine, hydrazine, and oxime-bond formation have been successfully used for accessing N-heterocyclic carbene platinum bioconjugate complexes. Among all the synthesized compounds, oxime-containing complexes were found to display a high hydrolytic stability and were found to be stable on silica gel or in wet solvents. As a proof of concept, the Pt NHC complexes were finally functionalized with three selective ligand-targeting moieties using oxime ligation. Preliminary results of the biological effects on various human cancer and non-cancer cells are also reported.

A metal-free synthetic approach to peptide-based iminosugar clusters as novel multivalent glycosidase inhibitors

Multivalent bioconjugates represent emerging tools for enzyme inhibition. In particular, iminosugar clusters have recently shown promising results for the inhibition of glycosidases. However, most of them are prepared by copper-mediated click reactions. We report herein a metal-free approach based on oxime ligation for preparing iminosugar clusters using cyclic and linear tetra-aldehyde peptide scaffolds and oxyamine iminosugars (40-70% yield). Glycosidase inhibition assays revealed the superiority of the clusters made of the linear scaffold, displaying up to a 77-fold increase of relative potency per iminosugar. Thus, this metal-free approach provides a rapid access to structurally-diverse iminosugar clusters for establishing structure-activity relationships in the context of multivalent glycosidase inhibition.

Synthesis, Radiosynthesis, and in vitro Studies on Novel Hypoxia PET Tracers Incorporating [18F]FDR

We report the synthesis of five radiotracers incorporating different oxyamine spacers between the hypoxia-reactive 2-nitroimidazole moiety and the 5-[18F]-fluorodeoxyribose ([18F]FDR, 12) prosthetic group: three linear alkyl chains w

Synthesis method for derivatization reagent containing carbonyl steroid compound (by machine translation)

The invention relates to a synthesis method for a carbonyl steroid compound derivatization reagent, and belongs to the technical field of chemical synthesis. The synthesis method comprises the following steps: firstly using 1,3 - dibromopropane and N - hydroxyphthalimide to react and synthesize 2 - (3 - bromopropoxy) isoindoline -1, 3 - diketone. 2 - (3 - Bromopropoxy) isoindoline -1, 3 - diketone was reused to prepare 3 - ((1,3 - dioxo -2 - isoindolinyl)-oxy) - N, N, N - trimethyl propyl ammonium bromide. Finally, hydrazinolysis of 3 - ((1,3 - dioxo -2 - isoindolyl)-oxy) - N, N, N - trimethylammonium bromide. The synthesis method is low in cost. The method has the advantages of simple steps, high yield, derivatization of the carbonyl steroid containing compounds, and introduction of the permanent charged groups - N therein. + Me3 , The detection sensitivity of the carbonyl steroid compound in ESI-MS / MS is improved. (by machine translation)

Chemoselective and Site-Selective Lysine-Directed Lysine Modification Enables Single-Site Labeling of Native Proteins

The necessity for precision labeling of proteins emerged during the efforts to understand and regulate their structure and function. It demands selective attachment of tags such as affinity probes, fluorophores, and potent cytotoxins. Here, we report a method that enables single-site labeling of a high-frequency Lys residue in the native proteins. At first, the enabling reagent forms stabilized imines with multiple solvent-accessible Lys residues chemoselectively. These linchpins create the opportunity to regulate the position of a second Lys-selective electrophile connected by a spacer. Consequently, it enables the irreversible single-site labeling of a Lys residue independent of its place in the reactivity order. The user-friendly protocol involves a series of steps to deconvolute and address chemoselectivity, site-selectivity, and modularity. Also, it delivers ordered immobilization and analytically pure probe-tagged proteins. Besides, the methodology provides access to antibody-drug conjugate (ADC), which exhibits highly selective anti-proliferative activity towards HER-2 expressing SKBR-3 breast cancer cells.

Single-site labeling of histidine in proteins, on-demand reversibility, and traceless metal-free protein purification

A precision methodology distinguishes one His from all the nucleophilic residues and its multiple copies. An easy-to-operate C-N bond formation labels diverse proteins without adversely affecting their structure and function. The late-stage transformation allows installation of distinct probes. The chemically triggered reversibility enables traceless metal-free purification of proteins with a His-tag.

HEMIAMINAL-TAG FOR PROTEIN LABELING AND PURIFICATION

The invention pertains to the synthesis, isolation, and characterization of hemiaminal for selective labeling of peptides, proteins, antibodies, and organic fragments with -C(=0) CH2NH2 and derivatives with -CH2NH2 group over -C(=0) CHRNH2 group (where R≠H). The invention also pertains to the method of single-site immobilization of proteins through N-terminus Gly on solid phase. The invention includes late-stage tagging of N-terminus Gly with an affinity tag, 19F NMR probe, and a fluorophore and a method for metal-free protein purification and isolation of analytically pure proteins.

Single-site labeling of lysine in proteins through a metal-free multicomponent approach

We report a chemoselective and site-selective approach that distinguishes one Lys from its multiple copies, N-terminus, and other competitors. The phospha-Mannich protocol works with multiple proteins and installs probes without structural and functional

Single-Site Labeling of Native Proteins Enabled by a Chemoselective and Site-Selective Chemical Technology

Chemical biology research often requires precise covalent attachment of labels to the native proteins. Such methods are sought after to probe, design, and regulate the properties of proteins. At present, this demand is largely unmet due to the lack of empowering chemical technology. Here, we report a chemical platform that enables site-selective labeling of native proteins. Initially, a reversible intermolecular reaction places the "chemical linchpins" globally on all the accessible Lys residues. These linchpins have the capability to drive site-selective covalent labeling of proteins. The linchpin detaches within physiological conditions and capacitates the late-stage installation of various tags. The chemical platform is modular, and the reagent design regulates the site of modification. The linchpin is a multitasking group and facilitates purification of the labeled protein eliminating the requirement of additional chromatography tag. The methodology allows the labeling of a single protein in a mixture of proteins. The precise modification of an accessible residue in protein ensures that their structure remains unaltered. The enzymatic activity of myoglobin, cytochrome C, aldolase, and lysozyme C remains conserved after labeling. Also, the cellular uptake of modified insulin and its downstream signaling process remain unperturbed. The linchpin directed modification (LDM) provides a convenient route for the conjugation of a fluorophore and drug to a Fab and monoclonal antibody. It delivers trastuzumab-doxorubicin and trastuzumab-emtansine conjugates with selective antiproliferative activity toward Her-2 positive SKBR-3 breast cancer cells.