Structural highlights
Function
[PLE1_PSEAM] Antimicrobial peptide with potent activity against Gram-positive and Gram-negative bacteria. Activity against E.coli and B.subtilis. Weaker activity against L.mucor, s.marcescens and P.aeruginosa. May play a role in innate host defense.
Publication Abstract from PubMed
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 (15)N-labeled peptide, a structure of pleurocidin was determined to be in a random coil conformation in aqueous solution whereas it assumes an alpha-helical structure in TFE and in dodecylphosphocholine (DPC) micelles. From (15)N 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.
Structural characterization of the antimicrobial peptide pleurocidin from winter flounder.,Syvitski RT, Burton I, Mattatall NR, Douglas SE, Jakeman DL Biochemistry. 2005 May 17;44(19):7282-93. PMID:15882067[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Syvitski RT, Burton I, Mattatall NR, Douglas SE, Jakeman DL. Structural characterization of the antimicrobial peptide pleurocidin from winter flounder. Biochemistry. 2005 May 17;44(19):7282-93. PMID:15882067 doi:10.1021/bi0504005
