Neutron reflection study of the interaction of the eukaryotic pore-forming actinoporin equinatoxin II with lipid membranes reveals intermediate states in pore formation
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- 作者：Hanna P. Wacklina ; b ; c ; Biserka Bakrač Bremecd ; Martina Moulinc ; Nejc Rojkod ; e ; Michael Haertleinc ; Trevor Forsythc ; Gregor Anderluhd ; e ; gregor.anderluh@ki.si" class="auth_mail" title="E-mail the corresponding author ; Raymond S. Nortonf ; ray.norton@monash.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Chol ; cholesterol ; DHPC ; dihexanoyl-phosphatidylcholine ; DMPC ; dimyristoyl-phosphatidylcholine ; DTT ; dithiothreitol ; EqtII ; equinatoxin II ; PC ; phosphatidylcholine ; SM ; sphingomyelin ; StII ; sticholysin II ; SUV ; small unilamellar vesicles
- 刊名：Biochimica et Biophysica Acta (BBA)-Biomembranes
- 出版年：2016
- 出版时间：April 2016
- 年：2016
- 卷：1858
- 期：4
- 页码：640-652
- 全文大小：2837 K
文摘
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Equinatoxin II has several modes of membrane binding depending on lipid composition.
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Equinatoxin II binds in a different orientation to DMPC–sphingomyelin compared with pure DMPC.
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Phase-separation promotes pore formation in DMPC–SM–cholesterol membranes.
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In situ release of the N-terminal α-helix confirms its role in pore formation.