Quantitative analyses of binding affinity and specificity for glycolipid receptors by surface plasmon resonance

In recent years, rapid expansion has been seen of the application of SPR to a wide range of biomolecular interactions. For protein-carbohydrate interactions, SPR techniques offer the means of presenting glycolipids, and potentially glycoproteins, in an environment that closely resembles their in vivo situation. It is already clear that the technology can provide much additional insight into these interactions because it monitors the interactions under conditions that approach physiologic ones and can allow for the investigation of parameters that are not accessible by conventional approaches. Strategies for the immobilization of glycolipids on BIACORE sensor chips are not limited to the two approaches described here. For example, liposomes containing biotinylated phospholipid could be captured by avidin or streptavidin surfaces; this strategy has been used for the capture of natural membrane vesicles. Also, Biacore AB has announced plans to introduce a version of the CM5 chip that has been derivatized with an undisclosed group that mediates the capture of large amounts of liposomes.