86770-72-1 Usage
Uses
Used in Bioconjugation:
Benzyl-PEG5-Azide is used as a linker for bioconjugation applications due to its ability to react with various functional groups and facilitate the formation of stable covalent bonds. This allows for the attachment of biological molecules, such as proteins, peptides, or nucleic acids, to other molecules or surfaces, which is crucial in the development of biosensors, drug delivery systems, and diagnostic tools.
Used in Drug Delivery Systems:
In the pharmaceutical industry, Benzyl-PEG5-Azide is used as a component in drug delivery systems to improve the solubility, stability, and bioavailability of therapeutic agents. The PEGylation of drugs can reduce their immunogenicity and increase their circulation time in the body, leading to enhanced therapeutic effects and reduced side effects.
Used in Materials Science:
Benzyl-PEG5-Azide is also utilized in materials science for the development of functional coatings, hydrogels, and other biocompatible materials. The incorporation of this linker allows for the attachment of specific biological molecules or chemical groups, enabling the creation of advanced materials with tailored properties for various applications, such as tissue engineering, regenerative medicine, and nanotechnology.
Check Digit Verification of cas no
The CAS Registry Mumber 86770-72-1 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 2 respectively.
Calculate Digit Verification of CAS Registry Number 86770-72:
(7*8)+(6*6)+(5*7)+(4*7)+(3*0)+(2*7)+(1*2)=171
171 % 10 = 1
So 86770-72-1 is a valid CAS Registry Number.
86770-72-1Relevant 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.
