Designer amphiphilic short peptides enhance thermal stability of isolated photosystem-I.
Designer amphiphilic short peptides enhance thermal stability of isolated photosystem-I.
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设计两亲性短肽增强孤立光系统-I 的热稳定性
DOI：
10.1371/journal.pone.0010233
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发表时间：
2010-04-21
期刊：
影响因子：
3.7
通讯作者：
Xu H
中科院分区：
文献类型：
--
作者：
Ge B;Yang F;Yu D;Liu S;Xu H
膜蛋白的稳定性在蛋白质纯化和结晶过程中以及在基于蛋白质的装置的制造中是至关重要的。最近的几项研究已经研究了各种表面活性剂如何稳定膜蛋白脱离其天然膜环境。然而，仍然没有一种表面活性剂可以普遍用于所有的膜蛋白。由于缺乏对表面活性剂和膜蛋白之间相互作用的了解，因此选择用于特定膜蛋白的表面活性剂仍然纯粹是经验性的。在这里，我们报告了一组短的两亲性肽提高多结构域蛋白质复合物光系统-I（PS-I）在水溶液中的热稳定性，肽表面活性剂具有明显的优势，比其他常用的烷基链为基础的表面活性剂。在所研究的所有短肽中，Ac-I5 K2-CONH 2（I5 K2）通过在0.65mM的浓度下将PS-I的解链温度从48.0°C提高到53.0°C并且显著延长分离的PS-I的半衰期而显示出最佳的稳定效果。AFM实验表明，PS-I/I5 K2/Triton X-100形成了大而稳定的囊泡，从而提供了模拟天然膜的界面环境，这可能部分解释了I5 K2增强PS-I热稳定性的原因。IxKy的亲水基和疏水基长度对PS-I的稳定性有重要影响。我们的研究结果表明，较长的疏水基团更有效地稳定PS-I。因此，这些简单的短肽在膜蛋白研究中具有重要的应用潜力。
Stability of membrane protein is crucial during protein purification and crystallization as well as in the fabrication of protein-based devices. Several recent studies have examined how various surfactants can stabilize membrane proteins out of their native membrane environment. However, there is still no single surfactant that can be universally employed for all membrane proteins. Because of the lack of knowledge on the interaction between surfactants and membrane proteins, the choice of a surfactant for a specific membrane protein remains purely empirical. Here we report that a group of short amphiphilic peptides improve the thermal stability of the multi-domain protein complex photosystem-I (PS-I) in aqueous solution and that the peptide surfactants have obvious advantages over other commonly used alkyl chain based surfactants. Of all the short peptides studied, Ac-I5K2-CONH2 (I5K2) showed the best stabilizing effect by enhancing the melting temperature of PS-I from 48.0°C to 53.0°C at concentration of 0.65 mM and extending the half life of isolated PS-I significantly. AFM experiments showed that PS-I/I5K2/Triton X-100 formed large and stable vesicles and thus provide interfacial environment mimicking that of native membranes, which may partly explain why I5K2 enhanced the thermal stability of PS-I. Hydrophobic and hydrophilic group length of IxKy had an important influence on the stabilization of PS-I. Our results showed that longer hydrophobic group was more effective in stabilizing PS-I. These simple short peptides therefore exhibit significant potential for applications in membrane protein studies.
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影响因子：
3.5
作者：
SHUBIN, VV;TSUPRUN, VL;KARAPETYAN, NV
通讯作者：
KARAPETYAN, NV
自组装肽洗涤剂会在干燥的表面上稳定孤立的光系统I。
影响因子：
9.8
作者：
通讯作者：
--
影响因子：
64.8
作者：
Amunts, Alexey;Drory, Omri;Nelson, Nathan
通讯作者：
Nelson, Nathan
影响因子：
4.3
作者：
Brettel, K;Leibl, W;Liebl, U
通讯作者：
Liebl, U
影响因子：
46.9
作者：
Bieri, C;Ernst, OP;Vogel, H
通讯作者：
Vogel, H