86770-73-2 Usage
General Description
Benzyl-PEG6-azide is a chemical compound consisting of a benzyl group, a polyethylene glycol (PEG) linker containing six ethylene glycol units, and an azide functional group. The benzyl group provides hydrophobic properties, while the PEG linker provides water solubility and flexibility. The azide functional group is a versatile chemical moiety commonly used in click chemistry reactions for the conjugation and modification of biomolecules and other compounds. Benzyl-PEG6-azide has applications in bioconjugation, drug delivery, surface modification, and materials science, due to its ability to selectively and efficiently react with alkyne groups using click chemistry. It is an important reagent in the field of chemical biology and drug discovery, where precise and controlled chemical modification and labeling of biomolecules is required.
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 articles and documents
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.
