1026270-95-0

Basic information

• Product Name: [2-(2-decyloxyethoxy)ethylsulfanylmethyl]benzene
• Synonyms: [2-(2-decyloxyethoxy)ethylsulfanylmethyl]benzene
• CAS NO: 1026270-95-0
• Molecular Weight: 352.582
• Mol File: 1026270-95-0.mol

Chemical Properties

• CAS DataBase Reference: [2-(2-decyloxyethoxy)ethylsulfanylmethyl]benzene(CAS DataBase Reference)
• NIST Chemistry Reference: [2-(2-decyloxyethoxy)ethylsulfanylmethyl]benzene(1026270-95-0)
• EPA Substance Registry System: [2-(2-decyloxyethoxy)ethylsulfanylmethyl]benzene(1026270-95-0)

Safety Data

• Hazardous Substances Data: 1026270-95-0(Hazardous Substances Data)

Upstream product

• 112-29-8 1-bromo dodecane 
• 1026096-30-9 2-(2-benzylsulfanylethoxy)ethanol 
• 100-53-8 phenylmethanethiol 

Relevant articles and documents

Carbohydrate-protein interactions at interfaces: Comparison of the binding of Ricinus communis lectin to two series of synthetic glycolipids using surface plasmon resonance studies

Two C-lactosyl lipids and the related C-galactosyl lipids have been synthesised and their binding to RCA120 plant lectin was compared with a second series of thiolactosylethoxyalkanes. The interactions were measured quantitatively in real time by surface plasmon resonance (BIAcore) at a range of concentrations and temperatures from 5 to 30°C. The C-galactosyl lipid (1,3-dimethyl-5-[β-D-galactopyranosyl]-5-(4-octadecyloxybenzyl)pyrimidine-2 ,4,6-trione) bound much more weakly with a KA = 8.86 × 105 than the corresponding C-lactosyl lipid (1,3-dimethyl-5-[β-D-galactopyranosyl-(1 → 4)-β-D-glucopyranosyl]-5-(4-octadecyloxybenzyl)pyrimidine-2,4,6-trione) (KA = 2.31 × 107). The influence of the linker region of the two different series of lactosyl lipids was clearly demonstrated by the differences in the binding to RCA120 lectin. The changes in kinetic values and in the enthalpic and entropic contribution to the free energy of binding reflected the importance of the linker and the hydrocarbon anchor holding the synthetic glycolipids in the neomembrane.

Carbohydrate-protein interactions at interfaces: synthesis of thiolactosyl glycolipids and design of a working model for surface plasmon resonance.

Thiolactosyl lipids designed for carbohydrate-protein binding studies have been synthesised. One representative was selected for binding studies with a plant lectin RCA120, the agglutinin from Ricinus communis. The interactions were measured quantitatively in real time using a BIAcore surface plasmon resonance instrument. Removal of much of the galactose from the thiolactosyl lipid in situ with beta-galactosidase showed that the lectin binding was highly specific. A dissociation constant KD = 8.77 x 10(-8) M was measured for 1-[2-[2-(2-[beta-D-galactopyranosyl-(1-->4)-1-thio-beta-D -glucopyranosyl]ethoxy)ethoxy]ethoxy]octadecane 30 which is four orders of magnitude greater than that determined for binding to lactose in solution. A concentration of lactose of > 80 mM was required to block the lectin binding to thiolactosyl lipid in a neomembrane.