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Stability of protein-decorated mixed lipid membranes: The interplay of lipid-lipid lipid-protein and protein-protein interactions

机译:蛋白修饰的混合脂质膜的稳定性:脂质-脂质脂质-蛋白质和蛋白质-蛋白质相互作用的相互作用

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摘要

Membrane-associated proteins are likely to contribute to the regulation of the phase behavior of mixed lipid membranes. To gain insight into the underlying mechanism, we study a thermodynamic model for the stability of a protein-decorated binary lipid layer. Here, proteins interact preferentially with one lipid species and thus locally sequester that species. We aim to specify conditions that lead to an additional macroscopic phase separation of the protein-decorated lipid membrane. Our model is based on a standard mean-field lattice-gas description for both the lipid mixture and the adsorbed protein layer. Besides accounting for the lipid-protein binding strength, we also include attractive lipid-lipid and protein-protein interactions. Our analysis characterizes the decrease in the membrane’s critical interaction parameter as a function of the lipid-protein binding strength. For small and large binding strengths we provide analytical expressions; numerical results cover the intermediate range. Our results reiterate the crucial importance of the line tension associated with protein-induced compositional gradients and the presence of attractive lipid-lipid interactions within the membrane. Direct protein-protein attraction effectively increases the line tension and thus tends to further destabilize the membrane.
机译:膜相关蛋白可能有助于调节混合脂质膜的相行为。为了深入了解潜在的机制,我们研究了蛋白质修饰的二元脂质层稳定性的热力学模型。在此,蛋白质优先与一种脂质物质相互作用,从而局部隔离该脂质物质。我们的目的是指定导致蛋白质修饰脂质膜发生宏观宏观相分离的条件。我们的模型基于脂质混合物和吸附蛋白层的标准平均场晶格气体描述。除了考虑脂质-蛋白质结合强度外,我们还包括有吸引力的脂质-脂质和蛋白质-蛋白质相互作用。我们的分析表明,膜的关键相互作用参数的降低是脂蛋白结合强度的函数。对于大大小小的结合强度,我们提供了分析表达式;数值结果涵盖了中间范围。我们的结果重申了与蛋白质诱导的成分梯度和膜内有吸引力的脂质-脂质相互作用的存在相关的线张力的至关重要性。直接的蛋白质-蛋白质吸引有效地增加了线张力,因此趋于进一步破坏膜的稳定性。

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