57671-28-0 Usage
Description
2-[2-[2-[2-[2-(BENZYLOXY)ETHOXY]ETHOXY]ETHOXY]ETHOXY]ETHANOL, also known as Benzyl-PEG6-alcohol, is a PEG (polyethylene glycol) linker with a benzyl protecting group and a primary alcohol. The benzyl protecting group can be removed under acidic conditions, and the primary alcohol allows for further derivatization of the compound. The hydrophilic PEG linker enhances the water solubility of the compound in aqueous media, making it suitable for various applications.
Uses
Used in Pharmaceutical Industry:
Benzyl-PEG6-alcohol is used as a solubility enhancer for poorly water-soluble drugs, improving their bioavailability and efficacy. The hydrophilic PEG linker increases the water solubility of the compound, allowing for better dispersion and absorption in the body.
Used in Chemical Synthesis:
Benzyl-PEG6-alcohol serves as a versatile building block in the synthesis of various chemical compounds, including pharmaceuticals, agrochemicals, and materials. The primary alcohol group enables further derivatization, allowing for the creation of a wide range of molecules with different properties and applications.
Used in Drug Delivery Systems:
In the field of drug delivery, Benzyl-PEG6-alcohol can be used as a component in the design of targeted drug delivery systems. The PEG linker can improve the solubility and stability of drug molecules, while the benzyl protecting group can be removed under specific conditions to release the active drug.
Used in Bioconjugation:
Benzyl-PEG6-alcohol can be employed in bioconjugation processes, where it can be used to attach biologically active molecules, such as peptides, proteins, or nucleic acids, to other molecules or surfaces. The primary alcohol group allows for covalent attachment, while the PEG linker provides stability and solubility benefits.
Used in Surface Modification:
In materials science, Benzyl-PEG6-alcohol can be utilized for surface modification of various substrates, such as nanoparticles, polymers, or solid supports. The PEG linker can improve the hydrophilicity and biocompatibility of the surface, while the benzyl protecting group can be removed to reveal functional groups for further modification or attachment of other molecules.
Check Digit Verification of cas no
The CAS Registry Mumber 57671-28-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,7,6,7 and 1 respectively; the second part has 2 digits, 2 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 57671-28:
(7*5)+(6*7)+(5*6)+(4*7)+(3*1)+(2*2)+(1*8)=150
150 % 10 = 0
So 57671-28-0 is a valid CAS Registry Number.
InChI:InChI=1/C17H28O6/c18-6-7-19-8-9-20-10-11-21-12-13-22-14-15-23-16-17-4-2-1-3-5-17/h1-5,18H,6-16H2
57671-28-0Relevant articles and documents
IRAK DEGRADERS AND USES THEREOF
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Paragraph 2050; 2051, (2019/07/10)
The present invention provides compounds, compositions thereof, and methods of using the same.
Homo-PROTACs: Bivalent small-molecule dimerizers of the VHL E3 ubiquitin ligase to induce self-degradation
Maniaci, Chiara,Hughes, Scott J.,Testa, Andrea,Chen, Wenzhang,Lamont, Douglas J.,Rocha, Sonia,Alessi, Dario R.,Romeo, Roberto,Ciulli, Alessio
, (2017/10/16)
E3 ubiquitin ligases are key enzymes within the ubiquitin proteasome system which catalyze the ubiquitination of proteins, targeting them for proteasomal degradation. E3 ligases are gaining importance as targets to small molecules, both for direct inhibition and to be hijacked to induce the degradation of non-native neo-substrates using bivalent compounds known as PROTACs (for 'proteolysis-targeting chimeras'). We describe Homo-PROTACs as an approach to dimerize an E3 ligase to trigger its suicide-type chemical knockdown inside cells. We provide proof-of-concept of Homo-PROTACs using diverse molecules composed of two instances of a ligand for the von Hippel-Lindau (VHL) E3 ligase. The most active compound, CM11, dimerizes VHL with high avidity in vitro and induces potent, rapid and proteasome-dependent self-degradation of VHL in different cell lines, in a highly isoform-selective fashion and without triggering a hypoxic response. This approach offers a novel chemical probe for selective VHL knockdown, and demonstrates the potential for a new modality of chemical intervention on E3 ligases.
Design and synthesis of novel hydrophilic spacers for the reduction of nonspecific binding proteins on affinity resins
Shiyama, Takaaki,Furuya, Minoru,Yamazaki, Akira,Terada, Tomohiro,Tanaka, Akito
, p. 2831 - 2841 (2007/10/03)
Tubulin and actin often bind nonspecifically to affinity chromatography resins, complicating research toward identifying the cellular targets. Reduction of nonspecific binding proteins is important for success in finding such targets. We herein disclose the design, synthesis, and effectiveness in reduction of nonspecific binding proteins, of novel hydrophilic spacers (2-5), which were introduced between matrices and a ligand. Among them, tartaric acid derivative (5) exhibited the most effective reduction of nonspecific binding proteins, whilst maintaining binding of the target protein. Introduction of 5 on TOYOPEARL reduced tubulin and actin by almost 65% and 90% compared to that without the hydrophilic spacer, respectively, with effective binding to the target protein, FKBP12.