Structure and dynamics of the antimicrobial peptide piscidin

CHED 920

Breanna S Vollmar, vollmabs@plu.edu1, Myriam Cotten, cottenml@plu.edu1, and Riqiang Fu, rfu@magnet.fsu.edu2. (1) Department of Chemistry, Pacific Lutheran University, Tacoma, WA 98447, (2) Department of Chemistry and Biochemistry, and National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL 32306-4390
Piscidin 3 is an amphipathic cationic histidine-rich antimicrobial peptide discovered in hybrid striped bass. The structure and dynamics of the peptide were investigated using several solid-state NMR techniques on both oriented and unoriented peptide-lipid samples. Rotational Echo DOuble Resonance conducted on piscidin 3 to characterize distances between residues located at positions 16 and 20 indicates that the peptide is alpha helical. 2-D Polarization Inversion Spin Exchange at the Magic Angle (PISEMA) experiments were performed on piscidin 3 in the presence of hydrated lipid bilayers to characterize the 15N chemical shift (CS) and 15N-1H dipolar coupling (DC) at positions 6, 9, 12, and 20. The best fit for the combined PISEMA data yields a tilt of 88.5 degrees for the orientation of the peptide with respect to the bilayer normal. The principles of molecular recognition emerging from these studies may help to develop low toxicity and highly efficient pharmaceuticals.
 

Undergraduate Research Poster Session: Biochemistry
2:00 PM-4:00 PM, Monday, March 26, 2007 Hyatt Regency Chicago -- Riverside Center, Poster

Division of Chemical Education

The 233rd ACS National Meeting, Chicago, IL, March 25-29, 2007