Membrane Interaction of Chrysophsin-1, a Histidine-Rich Antimicrobial Peptide from Red Sea Bream

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• 作者：A. James Mason ; Philippe Bertani ; Gilles Moulay ; Arnaud Marquette ; Barbara Perrone ; Alex F. Drake ; Antoine Kichler ; Burkhard Bechinger
• 刊名：Biochemistry
• 出版年：2007
• 出版时间：December 25, 2007
• 年：2007
• 卷：46
• 期：51
• 页码：15175 - 15187
• 全文大小：890K
• 年卷期：v.46,no.51(December 25, 2007)
• ISSN：1520-4995

文摘

Chrysophsin-1 is an amphipathic -helical antimicrobial peptide produced in the gill cells ofred sea bream. The peptide has broad range activity against both Gram-positive and Gram-negative bacteriabut is more hemolytic than other antimicrobial peptides such as magainin. Here we explore the membraneinteraction of chrysophsin-1 and determine its toxicity, in vitro, for human lung fibroblasts to obtain amechanism for its antimicrobial activity and to understand the role of the unusual C-terminal RRRHsequence. At intermediate peptide concentrations, solid-state NMR methods reveal that chrysophsin-1 isaligned parallel to the membrane surface and the lipid acyl chains in mixed model membranes aredestabilized, thereby being in agreement with models where permeabilization is an effect of transientmembrane disruption. The C-terminal RRRH sequence was shown to have a large effect on the insertionof the peptide into membranes with differing lipid compositions and was found to be crucial for poreformation and toxicity of the peptide to fibroblasts. The combination of biophysical data and cell-basedassays suggests likely mechanisms involved in both the antibiotic and toxic activity of chrysophsins.