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

Abstract : 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.
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https://www.hal.inserm.fr/inserm-00110419
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Submitted on : Saturday, October 28, 2006 - 11:17:12 PM
Last modification on : Thursday, February 21, 2019 - 9:56:03 AM
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Peter Critchley, Nicolas Willand, Atvinder Rullay, David Crout. Carbohydrate-protein interactions at interfaces: synthesis of thiolactosyl glycolipids and design of a working model for surface plasmon resonance.. Organic and Biomolecular Chemistry, Royal Society of Chemistry, 2003, 1 (6), pp.928-38. ⟨10.1039/b306784j⟩. ⟨inserm-00110419⟩

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