Probing the interaction forces between hydrophobic peptides and supported lipid bilayers using AFM
Probing the interaction forces between hydrophobic peptides and supported lipid bilayers using AFM
复制标题
使用 AFM 探测疏水性肽和支持的脂质双层之间的相互作用力
DOI：
10.1002/jmr.837
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发表时间：
2007
影响因子：
2.7
通讯作者：
Y. Dufrêne
中科院分区：
文献类型：
--
作者：
G. André;R. Brasseur;Y. Dufrêne
尽管在过去十年中积累了大量有关倾斜肽的文献，但仍缺乏有关驱动其与脂膜相互作用的力量的直接信息。在这里，我们尝试使用原子力显微镜（AFM）来探索猿猴免疫缺陷病毒肽与由各种脂质（即二棕榈酰磷脂酰胆碱、二油酰磷脂酰胆碱、二油酰磷脂酸和二棕榈酰磷脂酰乙醇胺）组成的相分离支撑双层之间的相互作用力。将组氨酸标记的肽连接到以次氮基三乙酸酯和三乙二醇基团终止的 AFM 尖端上，这种方法有望确保 C 末端疏水结构域的最佳暴露。肽尖端和不同双层结构域之间记录的力-距离曲线总是显示出接近时的长程排斥和缩回时缺乏粘附，这与肽的疏水性形成鲜明对比。为了解释这种意想不到的行为，我们提出了一种机制，其中由于与肽尖端的强烈相互作用，脂质从双层中被拉出，这与从支撑双层中提取脂质所需的非常低的力一致。版权所有 © 2007 约翰·威利父子有限公司
Despite the vast body of literature that has accumulated on tilted peptides in the past decade, direct information on the forces that drive their interaction with lipid membranes is lacking. Here, we attempted to use atomic force microscopy (AFM) to explore the interaction forces between the Simian immunodeficiency virus peptide and phase‐separated supported bilayers composed of various lipids, i.e. dipalmitoylphosphatidylcholine, dioleoylphosphatidylcholine, dioleoylphosphatidic acid and dipalmitoylphosphatidylethanolamine. Histidine‐tagged peptides were attached onto AFM tips terminated with nitrilotriacetate and tri(ethylene glycol) groups, an approach expected to ensure optimal exposure of the C‐terminal hydrophobic domain. Force–distance curves recorded between peptide‐tips and the different bilayer domains always showed a long‐range repulsion upon approach and a lack of adhesion upon retraction, in marked contrast with the hydrophobic nature of the peptide. To explain this unexpected behaviour, we suggest a mechanism in which lipids are pulled out from the bilayer due to strong interactions with the peptide‐tip, in agreement with the very low force needed to extract lipids from supported bilayers. Copyright © 2007 John Wiley & Sons, Ltd.