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首页> 美国卫生研究院文献>Biophysical Journal >Effect of Variations in the Structure of a Polyleucine-Based α-Helical Transmembrane Peptide on Its Interaction with Phosphatidylethanolamine Bilayers
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Effect of Variations in the Structure of a Polyleucine-Based α-Helical Transmembrane Peptide on Its Interaction with Phosphatidylethanolamine Bilayers

机译：基于聚亮氨酸的α-螺旋跨膜肽结构变化对其与磷脂酰乙醇胺双层相互作用的影响

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High-sensitivity differential scanning calorimetry and Fourier transform infrared spectroscopy were used to study the interaction of a cationic α-helical transmembrane peptide, acetyl-Lys2-Leu24-Lys2-amide (L24), and members of the homologous series of zwitterionic n-saturated diacyl phosphatidylethanolamines (PEs). Analogs of L24, in which the lysine residues were replaced by 2,3-diaminopropionic acid (acetyl-DAP2-Leu24-DAP2-amide (L24DAP)) or in which a leucine residue at each end of the polyleucine sequence was replaced by a tryptophan (Ac-K2-W-L22-W-K2-amide (WL22W)), were also studied to investigate the roles of lysine side-chain snorkeling and aromatic side-chain interactions with the interfacial region of phospholipid bilayers. The gel/liquid-crystalline phase transition temperature of the PE bilayers is altered by these peptides in a hydrophobic mismatch-independent manner, in contrast to the hydrophobic mismatch-dependent manner observed previously with zwitterionic phosphatidylcholine (PC) and anionic phosphatidylglycerol (PG) bilayers. Moreover, all three peptides reduce the phase transition temperature to a greater extent in PE bilayers than in PC and PG bilayers, indicating a greater disruption of PE gel-phase bilayer organization. Moreover, the lysine-anchored L24 reduces the phase transition temperature, enthalpy, and the cooperativity of PE bilayers to a much greater extent than DAP-anchored L24DAP, whereas replacement of the terminal leucines by tryptophan residues (Ac-K2-W-L22-W-K2-amide) only slightly attenuates the effects of this peptide on the chain-melting phase transition of the host PE bilayers. All three peptides form very stable α-helices in PE bilayers, but small conformational changes occur in response to mismatch between peptide hydrophobic length and gel-state lipid bilayer hydrophobic thickness. These results suggest that the lysine snorkeling plays a significant role in the peptide-PE interactions and that cation-π-interactions between lysine and tryptophan residues may modulate these interactions. Altogether, these results suggest that the lipid-peptide interactions are affected not only by the hydrophobic mismatch between these peptides and the host lipid bilayer but also by the electrostatic and hydrogen-bonding interactions between the positively charged lysine residues at the termini of these peptides and the polar headgroups of PE bilayers.
机译：高灵敏度差示扫描量热法和傅里叶变换红外光谱用于研究阳离子α-螺旋跨膜肽，乙酰基-Lys2-Leu24-Lys2-酰胺（L24）以及两性离子n-饱和同系物的相互作用二酰基磷脂酰乙醇胺（PEs）。 L24的类似物，其中赖氨酸残基被2,3-二氨基丙酸取代（乙酰基-DAP2-Leu24-DAP2-酰胺（L24DAP）），或多亮氨酸序列两端的亮氨酸残基被色氨酸取代（Ac-K2-W-L22-W-K2-酰胺（WL22W））也进行了研究，以研究赖氨酸侧链浮潜和芳香族侧链与磷脂双层界面区域的相互作用。这些肽以疏水错配非依赖性方式改变了PE双层的凝胶/液晶相变温度，这与以前两性离子磷脂酰胆碱（PC）和阴离子磷脂酰甘油（PG）双层所观察到的疏水错配依赖性方式相反。此外，与PC和PG双层相比，PE双层中的所有三种肽均将相变温度降低的程度更大，表明对PE凝胶相双层结构的破坏更大。而且，与DAP锚定的L24DAP相比，赖氨酸锚定的L24降低了PE双层的相变温度，焓和协同作用，而色氨酸残基取代了末端亮氨酸（Ac-K2-WL 22 -WK 2 -酰胺）仅略微减弱该肽对宿主PE双层链熔化相转变的影响。所有这三种肽在PE双层中均形成非常稳定的α螺旋，但响应于肽疏水长度和凝胶态脂质双层疏水厚度之间的不匹配，会发生小的构象变化。这些结果表明，赖氨酸浮潜在肽-PE相互作用中起重要作用，并且赖氨酸和色氨酸残基之间的阳离子-π相互作用可调节这些相互作用。总而言之，这些结果表明脂质-肽相互作用不仅受到这些肽与宿主脂质双层之间的疏水错配的影响，而且还受到这些肽末端的带正电荷的赖氨酸残基之间的静电和氢键相互作用的影响。 PE双层的极性头基。

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