1260001-87-3

Usage

Uses

Used in Chemical Biology:
Benzyl-PEG2-Azide is used as a versatile building block for the synthesis of bioconjugates and probes in chemical biology. The azide group allows for efficient and selective ligation with other molecules through copper-catalyzed Click Chemistry, enabling the development of novel imaging agents, drug delivery systems, and diagnostic tools.
Used in Medicinal Chemistry:
In medicinal chemistry, Benzyl-PEG2-Azide is employed as a key component in the design and synthesis of drug candidates with improved pharmacokinetic properties. The PEG linker can enhance the solubility, stability, and bioavailability of therapeutic agents, while the acid-labile benzyl protecting group ensures controlled release and targeted delivery to specific tissues or cells.
Used in Drug Delivery Systems:
Benzyl-PEG2-Azide is used as a component in the development of drug delivery systems, particularly for targeted and controlled release applications. The acid-labile benzyl protecting group allows for the release of the active pharmaceutical ingredient in response to specific environmental conditions, such as pH or enzymatic activity, ensuring optimal therapeutic efficacy and minimizing side effects.
Used in Bioconjugation:
In the field of bioconjugation, Benzyl-PEG2-Azide serves as a valuable intermediate for the attachment of biologically relevant molecules, such as peptides, proteins, or nucleic acids, to other chemical entities. The azide group facilitates efficient and selective ligation through copper-catalyzed Click Chemistry, enabling the creation of novel conjugates with tailored properties and functions.
Used in Materials Science:
Benzyl-PEG2-Azide is also utilized in materials science for the fabrication of functional polymers and materials with specific properties. The PEG linker can improve the hydrophilicity, biocompatibility, and self-assembly behavior of the resulting materials, making them suitable for applications in tissue engineering, regenerative medicine, and nanotechnology.

Upstream product

• 150272-33-6 di(ethylene glycol)monobenzyl ether methanesulfonate 
• 100-39-0 benzyl bromide 
• 2050-25-1 diethylene glycol monobenzyl ether 
• 98627-22-6 2-<2-(phenylmethoxy)ethoxy>ethanol 4-methylbenzenesulfonate 

Relevant academic research and scientific papers

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.

Click-based synthesis and proteomic profiling of lipstatin analogues

Using click chemistry to enable both structural diversity and proteome profiling within a natural product derived library, two out of nineteen lipstatin analogues showed similar activity to Orlistat against fatty acid synthase (FAS), but with an improved

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.