1043426-13-6 Usage
Description
Aminooxy-PEG2-azide is a versatile chemical compound that features an azide and an aminooxy group. The aminooxy group is highly reactive and can form an oxime linkage with aldehyde or ketone groups, while the azide group allows for Click Chemistry reactions. Due to its reactivity and sensitivity, Aminooxy-PEG2-azide should be used immediately (within 1 week) after synthesis to ensure optimal performance.
Uses
Used in Bioconjugation:
Aminooxy-PEG2-azide is used as a bioconjugation agent for the attachment of biomolecules to other chemical entities. The aminooxy group forms a stable oxime linkage with aldehyde or ketone groups present on the target biomolecule, facilitating the formation of covalent bonds and enhancing the stability of the conjugate.
Used in Drug Delivery Systems:
In the pharmaceutical industry, Aminooxy-PEG2-azide is used as a component in drug delivery systems. Aminooxy-PEG2-azide can be employed to modify drug molecules or drug carriers, enabling the formation of stable conjugates with targeting ligands or other therapeutic agents. This enhances the drug's bioavailability, targeting, and overall therapeutic efficacy.
Used in Materials Science:
Aminooxy-PEG2-azide is utilized as a reactive building block in the development of novel materials. Aminooxy-PEG2-azide's ability to form oxime linkages and participate in Click Chemistry reactions allows for the creation of complex, well-defined structures with tailored properties for various applications, such as sensors, coatings, or advanced materials for electronics and energy storage.
Used in Chemical Synthesis:
In organic synthesis, Aminooxy-PEG2-azide serves as an intermediate or a reagent for the synthesis of complex organic molecules. Aminooxy-PEG2-azide's reactivity and functional groups enable the formation of new chemical bonds and the construction of intricate molecular architectures, which can be applied in the development of pharmaceuticals, agrochemicals, or other specialty chemicals.
Check Digit Verification of cas no
The CAS Registry Mumber 1043426-13-6 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,0,4,3,4,2 and 6 respectively; the second part has 2 digits, 1 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 1043426-13:
(9*1)+(8*0)+(7*4)+(6*3)+(5*4)+(4*2)+(3*6)+(2*1)+(1*3)=106
106 % 10 = 6
So 1043426-13-6 is a valid CAS Registry Number.
1043426-13-6Relevant articles and documents
Site-selective glycosylation of hemoglobin with variable molecular weight oligosaccharides: Potential alternative to PEGylation
Styslinger, Thomas J.,Zhang, Ning,Bhatt, Veer S.,Pettit, Nicholas,Palmer, Andre F.,Wang, Peng G.
, p. 7507 - 7515 (2012)
Poly(ethylene glycol) (PEG) conjugation (i.e., PEGylation) is a commonly used strategy to increase the circulatory half-life of therapeutic proteins and colloids; however, few viable alternatives exist to replicate its functions. Herein, we report a method for the rapid site-selective glycosylation of proteins with variously sized carbohydrates, up to a molecular weight (MW) of 10 000, thus serving as a potential alternative for PEGylation. More importantly, the method developed has two unique features. First, traditional protecting group strategies that typically accompany the modification of the carbohydrate fragments are circumvented, allowing for the facile site-selective glycosylation of a desired protein with variously sized glycans. Second, the methodology employed is not limited by oligosaccharide size; consequently, glycans of MW similar to that of PEG, used in the PEGylation of therapeutic proteins, can be employed. To demonstrate the usefulness of this technology, hemoglobin (Hb) was site-selectively glycosylated with a series of carbohydrates of increasing MW (from 504 to ～10 000). Hb was selected on the basis of the vast wealth of biochemical and biophysical knowledge present in the literature and because of its use as a precursor in the synthesis/formulation of artificial red blood cell substitutes. Following the successful site-selective glycosylation of Hb, the impact of increasing the glycan MW on Hb's biophysical properties was investigated in vitro.
