UNSPECIFIED. (2003) Carbohydrate-protein interactions at interfaces: synthesis of thiolactosyl glycolipids and design of a working model for surface plasmon resonance. ORGANIC & BIOMOLECULAR CHEMISTRY, 1 (6). pp. 928-938. ISSN 1477-0520

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Abstract

Thiolactosyl lipids designed for carbohydrate-protein binding studies have been synthesised. One representative was selected for binding studies with a plant lectin RCA(120), 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 K-D = 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.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	ORGANIC & BIOMOLECULAR CHEMISTRY
Publisher:	ROYAL SOC CHEMISTRY
ISSN:	1477-0520
Date:	2003
Volume:	1
Number:	6
Number of Pages:	11
Page Range:	pp. 928-938
Identification Number:	10.1039/b210672h
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/9871

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