86770-73-2 Usage
Uses
Used in Bioconjugation:
Benzyl-PEG6-azide is used as a bioconjugation agent for the selective and efficient modification of biomolecules. Its azide functional group allows for click chemistry reactions with alkyne groups, enabling the formation of stable and specific conjugates for various applications.
Used in Drug Delivery Systems:
In the pharmaceutical industry, Benzyl-PEG6-azide is utilized as a component in drug delivery systems. Its PEG linker enhances the solubility and bioavailability of drugs, while the azide group enables the attachment of therapeutic agents through click chemistry, improving the targeting and efficacy of drug delivery.
Used in Surface Modification:
Benzyl-PEG6-azide is employed as a surface modification agent in materials science. The hydrophobic benzyl group and hydrophilic PEG linker provide a balance of properties that can be used to modify the surface properties of various materials, such as improving biocompatibility or enhancing specific interactions.
Used in Chemical Biology Research:
In the field of chemical biology, Benzyl-PEG6-azide serves as a valuable reagent for the study of biomolecular interactions and the development of new chemical probes. Its ability to selectively modify biomolecules through click chemistry allows researchers to explore the structure-function relationships of proteins, nucleic acids, and other biological macromolecules.
Check Digit Verification of cas no
The CAS Registry Mumber 86770-73-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,6,7,7 and 0 respectively; the second part has 2 digits, 7 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 86770-73:
(7*8)+(6*6)+(5*7)+(4*7)+(3*0)+(2*7)+(1*3)=172
172 % 10 = 2
So 86770-73-2 is a valid CAS Registry Number.
86770-73-2Relevant academic research and scientific papers
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
Jain, Ahamindra,Huang, Shaw G.,Whitesides, George M.
, p. 5057 - 5062 (2007/10/02)
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.
