86770-75-4

Usage

Uses

Used in Pharmaceutical Industry:
2-(Benzyloxyethoxyethoxy)ethylamine is used as a starting material for the synthesis of various pharmaceuticals. Its unique structure allows it to be easily modified and incorporated into a wide range of drug molecules, making it a valuable tool in the development of new medications.
Used in Chemical Research:
2-(Benzyloxyethoxyethoxy)ethylamine is used as a building block in the synthesis of other complex chemicals. Its versatility and ability to be easily modified make it a valuable resource for researchers in the field of organic chemistry.
Used in Manufacturing:
2-(Benzyloxyethoxyethoxy)ethylamine is used in the production of various organic compounds. Its wide range of applications and ability to be used as a starting material for the synthesis of a variety of different compounds make it a valuable chemical for many industries.

Upstream product

• 86770-70-9 ((2-(2-(2-azidoethoxy)ethoxy)ethoxy)methyl)benzene 
• 55489-58-2 triethylene glycol monobenzyl ether 
• 84131-04-4 triethylene glycol monobenzyl tosyl ether 
• 100-39-0 benzyl bromide 
• 112-27-6 2,2'-[1,2-ethanediylbis(oxy)]bisethanol 
• 2050-25-1 diethylene glycol monobenzyl ether 
• 702701-70-0 methanesulfonic acid 2-[2-(2-benzyloxy-ethoxy)-ethoxy]-ethyl ester 

Downstream Products

• 881310-66-3 C₃₉H₆₅N₅O₁₃ 
• 881310-64-1 C₂₇H₄₉N₅O₅ 
• 881310-63-0 C₂₃H₄₁N₅O₅ 
• 881310-68-5 C₅₁H₉₇N₁₃O₉ 
• 881310-67-4 C₄₃H₈₁N₁₃O₉ 
• 881310-62-9 3-[{2-[2-(2-benzyloxy-ethoxy)-ethoxy]-ethyl}-(2-methoxycarbonyl-ethyl)-amino]-propionic acid methyl ester 

Relevant academic research and scientific papers

Influence of Linker Attachment Points on the Stability and Neosubstrate Degradation of Cereblon Ligands

Proteolysis targeting chimeras (PROTACs) hijacking the cereblon (CRBN) E3 ubiquitin ligase have emerged as a novel paradigm in drug development. Herein we found that linker attachment points of CRBN ligands highly affect their aqueous stability and neosubstrate degradation features. This work provides a blueprint for the assembly of future heterodimeric CRBN-based degraders with tailored properties.

A MedChem toolbox for cereblon-directed PROTACs

A modular chemistry toolbox was developed for cereblon-directed PROTACs. A variety of linkers was attached to a CRBN ligand via the 4-amino position of pomalidomide. We used linkers of different constitution to modulate physicochemical properties. We equipped one terminus of the linker with a set of functional groups, e.g. protected amines, protected carboxylic acids, alkynes, chloroalkanes, and protected alcohols, all of which are considered to be attractive for PROTAC design. We also highlight different opportunities for the expansion of the medicinal chemists' PROTAC toolbox towards heterobifunctional molecules, e.g. with biotin, fluorescent, hydrophobic and peptide tags.

A new way to do an old reaction: highly efficient reduction of organic azides by sodium iodide in the presence of acidic ion exchange resin

Organic azides are readily reduced to the corresponding amines by treatment with sodium iodide in the presence of acidic ion exchange resin. The process, optimal when performed at 40 °C and 200 mbar pressure on a rotatory evaporator, is extremely efficient, clean, and tolerant of a variety of functional groups.

N-ACYLETHANOLAMINE HYDROLYZING ACID AMIDASE (NAAA) INHIBITORS AND THEIR USE THEREOF

A compound is represented as Formula I, a tautomer thereof, a stereoisomer thereof, or a pharmaceutically acceptable salt thereof. Compounds of Formula I are inhibitors of N-acylethanolamine hydrolyzing acid amidase (NAAA). The present technology is directed to compounds, compositions, and methods to inhibit N-acylethanolamine hydrolyzing acid amidase and to treat N-acylethanolamine hydrolyzing acid amidase mediated conditions in a subject.

Lack of effect of the length of oligoglycine- and oligo(ethylene glycol)-derived para-substituents on the affinity of benzenesulfonamides for carbonic anhydrase II in solution

Using 1H NMR spectroscopy, values of T2 have been determined for the methylene protons of the oligoglycine moieties of para-substituted benzenesulfonamides having structures H2NO2SC6H4CO(Gly)(n)OH (n = 1-6) bound at the active site of bovine carbonic anhydrase II (CA, EC 4.2.1.1). These values have been correlated with measurements of dissociation constants of these complexes, in order to infer motion of these ligands when bound to the enzyme. Motion of glycines 1-3 (those closest to the aryl ring) is hindered by their proximity to the protein; motion of glycines 4-6 is relatively unhindered. Despite the restriction to motion inferred for glycines 1-3, the values of K(d) for the six compounds (n = 1-6, 1-6) are indistinguishable within experimental uncertainty (± 20%): K(d) in μM (n) 0.30 (1); 0.26 (2); 0.33 (3); 0.37 (4); 0.37 (5); 0.34 (6). There is, therefore, an unexpected compensation of the loss in conformational entropy on binding by another contributor to the free energy.

REDUCTION D'AZIDES EN AMINES PAR LE FORMIATE D'AMMONIUM PAR "TRANSFERT D'HYDROGENE CATALYSE" (CTH)

The azides are reduced to amines in very good yields by "Catalytic Transfer Hydrogenation" (CTH) using ammonium formate.