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首页> 外文期刊>Thermochimica Acta: An International Journal Concerned with the Broader Aspects of Thermochemistry and Its Applications to Chemical Problems >The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-AlaHis-Gly) (PADH) with DPPC model membranes: a DSC study
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The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-AlaHis-Gly) (PADH) with DPPC model membranes: a DSC study

机译：肽与扰乱的疏水/亲水序列（Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-AlaHis-Gly）（PADH）与DPPC模型膜的相互作用： DSC研究

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Depending on their hydrophobicity, peptides can interact differently with lipid membranes inducing dramatic modifications into their host systems. In the present paper, the interaction of a synthetic peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) model membranes has been investigated by differential scanning calorimetry (DSC), adopting three different experimental approaches. In the first, the peptide is forced to be included into the hydrocarbon region c of the lipid bilayer, by codissolving it with the lipid giving rise to mixed multilamellar vesicles-peptide systems; in the second, this system is passed through an extruder, thus producing large unilamellar vesicles-pep tide systems; in the third, it is allowed to interact with the external surface of the membrane. The whole of the DSC results obtained have shown that the incorporation of the peptide into the lipid bilayer by means of the first method induces a decrease in the enthalpy of the gel-liquid crystal transition of the membrane and a shift of the transition to the lower temperatures, thus resembling, in spite of its prevalently hydrophilic nature, the behavior of transbilayer hydrophobic peptides. The extrusion of these systems creates unilamellar vesicles free of peptides but of smaller size as evidenced by the decreased cooperativity of the transition. The peptide, added externally to the DPPC model membrane, has no effect on the phase behavior of the bilayer. These findings suggest that the effect of the interaction of scrambled hydrophobic/hydrophilic peptides into lipid bilayers strongly affects the thermotropic behavior of the host membrane depending on the preparation method of the lipid/peptide systems. The whole of the results obtained in the present paper can be useful in approaching studies of bioactive peptides/lipids systems. (C) 2002 Elsevier Science B.V. All rights reserved. [References: 27]
机译：取决于它们的疏水性，肽可以与脂质膜发生不同的相互作用，从而在其宿主系统中引起显着的修饰。在本文中，合成肽与扰乱的疏水/亲水序列（Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly）的相互作用（通过三种不同的实验方法，通过差示扫描量热法（DSC）研究了带有1,2-二棕榈酰-sn-甘油-3-磷酸胆碱（DPPC）模型膜的PADH）。首先，通过将肽与脂质共溶解，使肽被强制包含在脂质双层的烃区域c中，从而形成混合的多层囊泡-肽系统。在第二步中，该系统通过挤出机，从而产生大的单层囊泡-pep潮汐系统。第三，允许其与膜的外表面相互作用。所获得的全部DSC结果表明，通过第一种方法将肽掺入脂质双层中导致膜的凝胶-液晶转变的焓降低以及转变向更低的转变。尽管具有普遍的亲水性，但其温度仍类似于转双分子疏水肽的行为。这些系统的挤出产生了不含肽但具有较小尺寸的单层囊泡，这由过渡的协同作用降低所证明。从外部添加到DPPC模型膜的肽对双层的相行为没有影响。这些发现表明，取决于脂质/肽系统的制备方法，加扰的疏水/亲水肽相互作用成脂质双层的作用强烈影响宿主膜的热致行为。本文获得的全部结果可用于进行生物活性肽/脂质系统的研究。 （C）2002 Elsevier Science B.V.保留所有权利。 [参考：27]

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