American Chemical Society
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Structural Characterization of the Antimicrobial Peptide Pleurocidin from Winter Flounder

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journal contribution
posted on 2005-05-17, 00:00 authored by Raymond T. Syvitski, Ian Burton, Neil R. Mattatall, Susan E. Douglas, David L. Jakeman
Pleurocidin is an antimicrobial peptide that was isolated from the mucus membranes of winter flounder (Pseudopleuronectes americanus) and contributes to the initial stages of defense against bacterial infection. From NMR structural studies with the uniformly 15N-labeled peptide, a structure of pleurocidin was determined to be in a random coil conformation in aqueous solution whereas it assumes an α-helical structure in TFE and in dodecylphosphocholine (DPC) micelles. From 15N relaxation studies, the helix is a rigid structure in the membrane-mimicking environment. Strong NOESY cross-peaks from the pleurocidin to the aliphatic chain on DPC confirm that pleurocidin is contained within the DPC micelle and not associated with the surface of the micelle. From diffusion studies it was determined that each micelle contains at least two pleurocidin molecules.