ORGN 709 |
| The development of high affinity, sensitive, selective and robust ligands as integral components of biosensors is crucial for emerging detection technologies. In addition to antibodies, Nature uses carbohydrates to mediate a wide array of biological processes such as inflammation, cell – cell interactions, cell development, host – bacteria interactions and viral entry. Glycosylated ligands are often found as first docking sites of a pathogen with more specific secondary and later binding to protein recognition elements. Although glyco-protein interactions are often of low selectivity and the binding affinities are generally too low to capture a pathogen with a single binding event. This affinity limitation can be overcome by multivalent binding to several glycosidic ligands, further enhanced by surface avidity on a membrane or membrane like surface and targeting multiple receptor sites on a pathogen. In this poster, we present the synthesis of novel scaffolds and the covalent linkage of pathogen specific ligands to the scaffold. |
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Asymmetric Reactions, Combinatorial Chemistry, Molecular Recognition and Self-Assembly, Proteins, Peptides, Amino Acids and Enzyme Inhibitors
8:00 PM-10:00 PM, Wednesday, March 28, 2007 Hyatt Regency Chicago -- Riverside Center, Poster
Division of Organic Chemistry |