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 Glactosyl lipids and the related C-galactosyl lipids have been synthesised and their binding to RCA(120) 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 co...

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Bibliographic Details
Published in:Organic & biomolecular chemistry Vol. 1; no. 23; pp. 4148 - 4159
Main Authors: Critchley, P, Clarkson, GJ
Format: Journal Article
Language:English
Published: CAMBRIDGE Royal Soc Chemistry 07.12.2003
Subjects:
1,2-Dipalmitoylphosphatidylcholine - chemistry
1,2-Dipalmitoylphosphatidylcholine - metabolism
Binding Sites
Chemistry
Chemistry, Organic
Glycolipids - chemical synthesis
Glycolipids - chemistry
Glycolipids - metabolism
Hydrolysis
Ligands
Molecular Conformation
Molecular Structure
Physical Sciences
Protein Binding
Ricin - chemistry
Ricin - metabolism
Science & Technology
Surface Plasmon Resonance
Thermodynamics
GOLD
SELF-ASSEMBLED MONOLAYERS
ACID
THERMODYNAMIC ANALYSIS
CONVENIENT
GENERATION
C-GLYCOSIDES
MODEL
CONFORMATION
MONOSACCHARIDE
ISSN:1477-0520, 1477-0539
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Summary:Two Glactosyl lipids and the related C-galactosyl lipids have been synthesised and their binding to RCA(120) 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 30degreesC. The C-galactosyl lipid (1,3-dimethyl-5-[beta-D-galactopyranosyl]-5-(4-octadecyloxybenzyl)pyrimidine-2,4,6-trione) bound much more weakly with a K-A = 8.86 x 10(5) than the corresponding Glactosyl lipid (1,3-dimethyl-5-[beta-D-galactopyranosyl-(1-->4)-beta-D-glucopyranosyl]-5-(4-octadecyloxybenzyl)pyrimidine-2,4,6-trione) (K-A = 2.31 x 10(7)). The influence of the linker region of the two different series of lactosyl lipids was clearly demonstrated by the differences in the binding to RCA(120) 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.
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ISSN:1477-0520
1477-0539
DOI:10.1039/b306784j