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 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 degrees C. 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 C-lactosyl 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 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.
Critchley
P
P
Department of Chemistry, University of Warwick, Coventry, UK CV4 7AL. lonpobty@supanet.com
Clarkson
G J
GJ
D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D006017:Glycolipids / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D008024:Ligands; D008968:Molecular Conformation; D015394:Molecular Structure; D011485:Protein Binding; D012276:Ricin / Q000737:chemistry* / Q000378:metabolism*; D020349:Surface Plasmon Resonance; D013816:Thermodynamics
D006017:Glycolipids; D008024:Ligands; D015060:1,2-Dipalmitoylphosphatidylcholine; D012276:Ricin