Structural characterization of the antimicrobial peptide pleurocidin from winter flounder

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DOIResolve DOI: http://doi.org/10.1021/bi0504005
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TypeArticle
Journal titleBiochemistry
Volume44
Issue19
Pages72827293; # of pages: 12
Subjectantibodies; antimicrobial peptides; biological membranes; conformation; defence mechanisms; diffusion; fish physiology; infection; marine fish; micelles; mucus; N.M.R.; peptides; random coil; Pseudopleuronectes americanus
AbstractPleurocidin 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 -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.
Publication date
PublisherACS Publications
Copyright noticeCopyright © 2005 American Chemical Society
LanguageEnglish
AffiliationNational Research Council Canada; Aquatic and Crop Resource Development; NRC Institute for Marine Biosciences
Peer reviewedYes
NRC number42491
1448
NPARC number3538209
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Record identifier15e6d6eb-cb69-4146-a206-da219de67687
Record created2009-03-01
Record modified2016-05-09
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