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首页> 美国卫生研究院文献>Biophysical Journal >Morphological behavior of acidic and neutral liposomes induced by basic amphiphilic alpha-helical peptides with systematically varied hydrophobic-hydrophilic balance.
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Morphological behavior of acidic and neutral liposomes induced by basic amphiphilic alpha-helical peptides with systematically varied hydrophobic-hydrophilic balance.

机译：碱性两亲性α-螺旋肽诱导的酸性和中性脂质体的形态学行为系统地改变了疏水-亲水平衡。

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Lipid-peptide interaction has been investigated using cationic amphiphilic alpha-helical peptides and systematically varying their hydrophobic-hydrophilic balance (HHB). The influence of the peptides on neutral and acidic liposomes was examined by 1) Trp fluorescence quenched by brominated phospholipid, 2) membrane-clearing ability, 3) size determination of liposomes by dynamic light scattering, 4) morphological observation by electron microscopy, and 5) ability to form planar lipid bilayers from channels. The peptides examined consist of hydrophobic Leu and hydrophilic Lys residues with ratios 13:5, 11:7, 9:9, 7:11, and 5:13 (abbreviated as Hels 13-5, 11-7, 9-9, 7-11, and 5-13, respectively; Kiyota, T., S. Lee, and G. Sugihara. 1996. Biochemistry. 35:13196-13204). The most hydrophobic peptide (Hel 13-5) induced a twisted ribbon-like fibril structure for egg PC liposomes. In a 3/1 (egg PC/egg PG) lipid mixture, Hel 13-5 addition caused fusion of the liposomes. Hel 13-5 formed ion channels in neutral lipid bilayer (egg PE/egg PC = 7/3) at low peptide concentrations, but not in an acidic bilayer (egg PE/brain PS = 7/3). The peptides with hydrophobicity less than Hel 13-5 (Hels 11-7 and Hel 9-9) were able to partially immerse their hydrophobic part of the amphiphilic helix in lipid bilayers and fragment liposome to small bicelles or micelles, and then the bicelles aggregated to form a larger assembly. Peptides Hel 11-7 and Hel 9-9 each formed strong ion channels. Peptides (Hel 7-11 and Hel 5-13) with a more hydrophilic HHB interacted with an acidic lipid bilayer by charge interaction, in which the former immerses the hydrophobic part in lipid bilayer, and the latter did not immerse, and formed large assemblies by aggregation of original liposomes. The present study clearly showed that hydrophobic-hydrophilic balance of a peptide is a crucial factor in understanding lipid-peptide interactions.
机译：已经使用阳离子两亲性α-螺旋肽并系统地改变其疏水-亲水平衡（HHB）来研究脂质-肽之间的相互作用。通过1）溴化磷脂淬灭的Trp荧光，2）膜清除能力，3）通过动态光散射测定脂质体的大小，4）通过电子显微镜观察形态学和5检验了肽对中性和酸性脂质体的影响。 ）从通道形成平面脂质双层的能力。检查的肽由疏水性Leu和亲水性Lys残基组成，比率为13：5、11：7、9：9、7：11和5:13（缩写为Hels 13-5、11-7、9-9、7分别为-11和5-13； Kiyota，T.，S。Lee和G. Sugihara。1996. Biochemistry。35：13196-13204）。疏水性最强的肽（Hel 13-5）为卵PC脂质体诱导了扭曲的带状原纤维结构。在3/1（鸡蛋PC /鸡蛋PG）脂质混合物中，加入Hel 13-5会导致脂质体融合。 Hel 13-5在低肽浓度下在中性脂质双层中（例如PE / eg PC = 7/3）形成了离子通道，但在酸性双层中未形成离子通道（例如PE /大脑PS = 7/3）。疏水性小于Hel 13-5（Hels 11-7和Hel 9-9）的肽能够将其两亲螺旋的疏水部分部分浸入脂质双层中，并将脂质体片段化为小的Bicelles或胶束，然后Bicelles聚集形成更大的组件。肽Hel 11-7和Hel 9-9各自形成强离子通道。具有更高亲水性HHB的肽（Hel 7-11和Hel 5-13）通过电荷相互作用与酸性脂质双分子层相互作用，其中前者将疏水部分浸入脂质双分子层中，而后者没有浸入，并形成大型装配体通过聚集原始脂质体。本研究清楚地表明，肽的疏水-亲水平衡是理解脂质-肽相互作用的关键因素。

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