A hemocyanin-derived antimicrobial peptide from the penaeid shrimp adopts an alpha-helical structure that specifically permeabilizes fungal membranes
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- 作者：Vanessa W. Petita ; 1 ; Jean-Luc Rollandb ; Alain Blonda ; Chantal Cazevieilled ; Chakib Djediata ; Jean Peduzzia ; Christophe Goularda ; Evelyne Bachè ; reb ; Joë ; lle Dupontc ; Delphine Destoumieux-Garzó ; nb ; 2 ; Sylvie Rebuffata ; 2 ; rebuffat@mnhn.fr" class="auth_mail" title="E-mail the corresponding author
- 关键词：Antimicrobial peptide ; Amphipathic helix ; Fungi ; Membrane bilayer ; Nuclear magnetic resonance (NMR) ; Fluorescence microscopy
- 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
- 出版年：2016
- 出版时间：March 2016
- 年：2016
- 卷：1860
- 期：3
- 页码：557-568
- 全文大小：1476 K
文摘
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First description of a hemocyanin-derived antifungal peptide mechanism of action
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PvHCt is a histidine-rich antifungal peptide encrypted in shrimp hemocyanin.
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The hemocyanin-derived antifungal peptide folds into an alpha-helix.
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PvHCt binds to fungal cells and specifically permeabilizes fungal membranes.
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Fungal cell death results from specific peptide-induced fungal membrane damages.