ORGN 675 |
| Buforin II is a 21 amino acid, cationic antimicrobial peptide isolated from the stomach tissue of Asian toad Bufo bufo garagrizans in 1996. It is hypothesized to target bacteria nonspecifically by crossing biological membranes without membrane permeabilization and binding to DNA. Our research focuses on how lipid composition affects membrane binding and translocation of buforin II. To this end, we have used a fluorescence titration method to measure the binding of buforin II to lipid vesicles with varying compositions of phosphatidylglycerol, phosphatidylethanolamine, phosphatidylcholine, and phosphatidylserine. Current results suggest that the binding strength between buforin II and the lipid vesicles increases as the amount of negatively charged lipids increase. Molecular dynamics simulations have provided additional insight into these results. We have also adapted equilibrium dialysis and a biotin-avidin based protocol to measure buforin II translocation across lipid vesicles of varying composition.
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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
Sci-Mix
Division of Organic Chemistry |