928211-42-1

Basic information

• Product Name: PEG22
• Synonyms: PEG22;PEG21
• CAS NO: 928211-42-1
• Molecular Formula: C₄₂H₈₆O₂₂
• Molecular Weight: 943.12
• Mol File: 928211-42-1.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: PEG22(CAS DataBase Reference)
• NIST Chemistry Reference: PEG22(928211-42-1)
• EPA Substance Registry System: PEG22(928211-42-1)

Safety Data

• Hazardous Substances Data: 928211-42-1(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
PEG22 is used as a solubility enhancer for improving the water solubility of hydrophobic drugs, facilitating their absorption and bioavailability in the body. The increased solubility also aids in the formulation of drugs with better stability and performance.
Used in Cosmetics Industry:
In the cosmetics industry, PEG22 is utilized as an emulsifier and humectant. Its ability to form stable emulsions helps in creating homogenous mixtures of oil and water, while its humectant properties assist in retaining moisture within cosmetic products, ensuring their efficacy and longevity.
Used in Biomedical Research:
PEG22 is employed as a protein or peptide modifier in biomedical research. The hydroxyl groups enable covalent attachment of PEG22 to proteins or peptides, which can improve their stability, solubility, and circulation time in the body. This modification can also reduce immunogenicity and proteolytic degradation, making it a valuable tool in drug delivery and protein engineering.
Used in Chemical Synthesis:
In chemical synthesis, PEG22 serves as a versatile building block for the creation of various PEGylated compounds. Its reactive hydroxyl groups allow for the synthesis of PEG-based conjugates, copolymers, and other complex structures with tailored properties for specific applications in materials science, nanotechnology, and more.

Upstream product

• 57671-28-0 2-(2-{2-[2-(2-benzyloxyethoxy)ethoxy]ethoxy}ethoxy)ethanol 

Relevant articles and documents

Dependence of effective molarity on linker length for an intramolecular protein-ligand system

This paper reports dissociation constants and "effective molarities" (Meff) for the intramolecular binding of a ligand covalently attached to the surface of a protein by oligo(ethylene glycol) (EGn) linkers of different lengths (n = 0, 2, 5, 10, and 20) and compares these experimental values with theoretical estimates from polymer theory. As expected, the value of Meff is lowest when the linker is too short (n = 0) to allow the ligand to bind noncovalently at the active site of the protein without strain, is highest when the linker is the optimal length (n = 2) to allow such binding to occur, and decreases monotonically as the length increases past this optimal value (but only by a factor of ～8 from n = 2 to n = 20). These experimental results are not compatible with a model in which the single bonds of the linker are completely restricted when the ligand has bound noncovalently to the active site of the protein, but they are quantitatively compatible with a model that treats the linker as a random-coil polymer. Calorimetry revealed that enthalpic interactions between the linker and the protein are not important in determining the thermodynamics of the system. Taken together, these results suggest that the manifestation of the linker in the thermodynamics of binding is exclusively entropic. The values of Meff are, theoretically, intrinsic properties of the EGn linkers and can be used to predict the avidities of multivalent ligands with these linkers for multivalent proteins. The weak dependence of Meff on linker length suggests that multivalent ligands containing flexible linkers that are longer than the spacing between the binding sites of a multivalent protein will be effective in binding, and that the use of flexible linkers with lengths somewhat greater than the optimal distance between binding sites is a justifiable strategy for the design of multivalent ligands.