1026096-30-9Relevant academic research and scientific papers
Carbohydrate-protein interactions at interfaces: Comparison of the binding of Ricinus communis lectin to two series of synthetic glycolipids using surface plasmon resonance studies
Critchley,Clarkson
, p. 4148 - 4159 (2003)
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.
Efficient synthesis of methanesulphonate-derived lipid chains for attachment of proteins to lipid membranes
Hicks, Matthew R.,Rullay, Atvinder K.,Pedrido, Rosa,Crout, David H.,Pinheiro, Teresa J. T.
, p. 3726 - 3750 (2008/12/23)
We have developed an easy and flexible synthetic methodology to obtain lipid chains containing methanothiosulfonate terminal groups with the aim to attach them to natural proteins as functional groups. There are many proteins found in nature that are modified by lipids, and this is a key part of their function. For example, the prion protein is attached to the plasma membrane via a glycosylphosphatidylinositol (GPI) anchor, and this protein is thought to be the causative agent in diseases such as bovine spongiform encephalopathy (BSE; "mad cow disease") and the human equivalent Creutzfeldt-Jakob disease. However, production of large amounts of protein in bacteria results in proteins that lack these lipid modifications. The lipid chains containing methanothiosulfonate terminal groups that we have synthesized here can be attached to these proteins through the thiol contained in the side chain of the cysteine residue, which can be incorporated into the protein sequence at the desired position. Copyright Taylor & Francis Group, LLC.
Carbohydrate-protein interactions at interfaces: synthesis of thiolactosyl glycolipids and design of a working model for surface plasmon resonance.
Critchley, Peter,Willand, M Nicolas,Rullay, Atvinder K,Crout, David H
, p. 928 - 938 (2007/10/03)
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.
