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

被引:11
作者
Critchley, P [1 ]
Willand, MN [1 ]
Rullay, AK [1 ]
Crout, DHG [1 ]
机构
[1] Univ Warwick, Dept Chem, Coventry CV4 7AL, W Midlands, England
关键词
D O I
10.1039/b210672h
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
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.
引用
收藏
页码:928 / 938
页数:11
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