ORGN 756 |
| Periplasmic binding proteins (PBPs) are naturally occurring nanoscale biosensors, used by bacteria to sense a variety of small molecules in the environment. Each PBP binds selectively and with high affinity its target ligand, and the PBP family includes members targeting carbohydrates, amino acids and other organic amines. Despite the variety of targeted ligands, each PBP exhibits a similar, “venus-flytrap” conformational change upon ligand binding. Several labs have exploited this relatively large movement to create synthetic systems which give an optical or electrochemical readout when ligand is present. Our approach uses bioconjugation reactions developed in our lab to create a versatile, modular set of biosensors that can be readily incorporated into virtually any device of interest. A key feature of this strategy is the site-selective modification of the N-terminus using a biomimetic transamination reaction. This method can be carried out in buffered aqueous solution under mild pH and temperature conditions. The performance of these sensors and their incorporation into devices will be presented. |
|
Total Synthesis, Materials, Molecular Recognition, Process R&D, and Physical Organic Chemistry
8:00 PM-10:00 PM, Wednesday, 13 September 2006 Moscone Center -- Hall D, Poster
Sci-Mix
Division of Organic Chemistry |