title: Determination of glycolipid-protein interaction specificity.
abstract: Glycolipids are found on all eukaryotic cells. Their expression varies among tissues, with the highest density found in the brain, where glycolipids are the most abundant of all glycoconjugate classes. In addition to playing roles in membrane structure, glycolipids also act as cell surface recognition molecules, mediating cell-cell interactions, as well as binding certain pathogens and toxins. Because of their amphipathic nature, underivatized glycolipids are amenable to immobilization on hydrophobic surfaces, where they can be probed with lectins, antibodies, pathogens, toxins, and intact cells to reveal their binding specificities and affinities. Three particularly useful methods to probe specific glycolipid-mediated recognition events are microwell adsorption (ELISA), thin layer chromatography overlay, and surface plasmon resonance (SPR) spectroscopy.
authors.affiliation: Department of Neurology, John Hopkins University School of Medicine, Baltimore, Maryland, USA.
authors.forename: Pablo H H
authors.initials: PH
authors.lastname: Lopez
authors.forename: Ronald L
authors.initials: RL
authors.lastname: Schnaar
mesh_terms: D000818:Animals; D006017:Glycolipids / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding / Q000502:physiology; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D006017:Glycolipids; D011506:Proteins