Associate Professor of Chemistry Myriam Cotten published a paper in the Journal of the American Chemical Society, the flagship journal of the American Chemical Society. The paper titled “High Resolution Heteronuclear Correlation NMR Spectroscopy of an Antimicrobial Peptide in Aligned Lipid Bilayers: Peptide-Water Interactions at the Water-Bilayer Interface” is co-authored with two undergraduates as well as Dr. Riqiang Fu, a research scientist at the National High Magnetic Field Laboratory in Tallahassee.
The molecular system of interest in this research is piscidin, an antimicrobial peptide that recognizes microbial membranes as part of its mechanism of action. Using a Nuclear Magnetic Resonance (NMR) technique recently developed by Fu, Cotten and her students studied piscidin’s NMR signals at different magnetic field strengths and obtained improved resolution on the NHMFL 900 MHz instrument, the only ultra-wide bore ultra-high field superconducting NMR instrument in the world.
The paper also highlights the first direct evidence of peptide-water interactions in a sample containing hydrated lipid bilayers and a peptide. This result points at peptide-lipid interactions that may be related to the ability of antimicrobial peptides to disrupt bacterial membranes and induce cell death. The long term goal of the Cotten group is to identify common principles that will facilitate the design of pharmaceuticals with enhanced antibacterial activity.
The molecular system of interest in this research is piscidin, an antimicrobial peptide that recognizes microbial membranes as part of its mechanism of action. Using a Nuclear Magnetic Resonance (NMR) technique recently developed by Fu, Cotten and her students studied piscidin’s NMR signals at different magnetic field strengths and obtained improved resolution on the NHMFL 900 MHz instrument, the only ultra-wide bore ultra-high field superconducting NMR instrument in the world.
The paper also highlights the first direct evidence of peptide-water interactions in a sample containing hydrated lipid bilayers and a peptide. This result points at peptide-lipid interactions that may be related to the ability of antimicrobial peptides to disrupt bacterial membranes and induce cell death. The long term goal of the Cotten group is to identify common principles that will facilitate the design of pharmaceuticals with enhanced antibacterial activity.
