Hydrophobic interactions of peptides with membrane interfaces
Hydrophobic interactions of peptides with membrane interfaces
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DOI：
10.1016/s0304-4157(98)00021-5
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发表时间：
1998-11-10
期刊：
影响因子：
--
通讯作者：
Wimley, WC
中科院分区：
文献类型：
--
作者：
White, SH;Wimley, WC
由于与水相不溶性和膜相极端稳定性相关的棘手问题，膜蛋白结构稳定性的热力学原理很难直接从整个蛋白质中获得。因此，必须通过小肽与脂质双层相互作用的研究来推测其原理。本综述涉及此类肽与脂质双层界面区域的疏水相互作用。我们首先开发了一个以界面相互作用为中心的膜蛋白稳定性热力学思考的通用框架，并回顾了支持这种以界面为中心的观点的结构和化学证据。然后，我们描述了通过实验确定的全残基界面疏水性尺度，该尺度揭示了肽键在分配和折叠中的核心作用。最后，我们考虑了使用不同类别的肽确定的侧链疏水性之间的差异所揭示的界面相互作用的复杂性和多样性。 (C) 1998 Elsevier Science B.V. 保留所有权利。
The thermodynamic principles underlying the structural stability of membrane proteins are difficult to obtain directly from whole proteins because of intractable problems related to insolubility in the aqueous phase and extreme stability in the membrane phase. The principles must therefore be surmised from studies of the interactions of small peptides with lipid bilayers. This review is concerned with the hydrophobic interactions of such peptides with the interfacial regions of lipid bilayers. We first develop a general framework for thinking about the thermodynamics of membrane protein stability that centers on interfacial interactions and review the structural and chemical evidence that supports this interface-centered point of view. We then describe an experimentally determined whole-residue interfacial hydrophobicity scale that reveals the central role of the peptide bond in partitioning and folding. Finally, we consider the complexity and diversity of interfacial interactions revealed by differences between side-chain hydrophobicities determined using different classes of peptides. (C) 1998 Elsevier Science B.V. All rights reserved.