Metal-directed protein self-assembly.
Metal-directed protein self-assembly.
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DOI：
10.1021/ar900273t
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发表时间：
2010-05-18
影响因子：
18.3
通讯作者：
Tezcan, F. Akif
中科院分区：
文献类型：
--
作者：
Salgado, Eric N.;Radford, Robert J.;Tezcan, F. Akif
蛋白质是自然界构建复杂的纳米级结构的首要基石，这些结构可以执行复杂的任务和化学转化。据估计，所有蛋白质中有70-80%是永久寡聚的，也就是说，它们由多个蛋白质组成，这些蛋白质通过非共价相互作用以精确的空间组织结合在一起。虽然了解蛋白质自组装的物理化学基础是非常重要的，但掌握蛋白质-蛋白质相互作用（PPIs）也将允许使用大自然最喜欢和最通用的构建块获得新的生物材料。考虑到这种可能性，我们开发了一种新的方法，金属定向蛋白质自组装（MDPSA），它利用金属-配体相互作用的强度、方向性和选择性来控制PPIs。MDPSA的核心是受超分子配位化学的启发，该化学利用金属配位将小分子自组装成离散的、或多或少可预测的高阶结构。然而，蛋白质并不完全是小分子或简单的金属配体：它们具有广泛的、异质的表面，可以以不可预测的方式相互作用，也可以与金属离子相互作用。我们将通过首先描述使用整个蛋白质作为分子构建块的挑战来开始这个帐户。接下来，我们将对一种模型蛋白（细胞色素cb562）进行研究，以突出并克服这些挑战，为MDPSA建立一些基本规则。蛋白质也是大自然选择的金属配体。在MDPSA中，一旦金属离子引导蛋白质形成大型组件，它们就会被定义嵌入蛋白质表面之间形成的广泛界面中。这些复杂的表面使无机化学家的生活有些困难，但它们也提供了一个广泛的平台，通过远距离、非共价的相互作用来调节金属配位环境——就像天然金属蛋白和酶一样。我们将描述我们在重组界面金属中心周围蛋白质之间形成的非共价相互作用网络方面的计算和实验工作。这种金属模板化后再设计蛋白质界面的方法（metal - templated Interface redesign, MeTIR）不仅为设计全新的PPIs和新的金属配位环境提供了途径，而且还可能与金属蛋白的进化有相似之处。
Proteins are Nature’s premier building blocks for constructing sophisticated nanoscale architectures that carry out complex tasks and chemical transformations. It is estimated that 70–80% of all proteins are permanently oligomeric, that is, they are composed of multiple proteins that are held together in precise spatial organization through non-covalent interactions. While it is of great fundamental interest to understand the physicochemical basis of protein self-assembly, the mastery of protein-protein interactions (PPIs) would also allow access to novel biomaterials using Nature’s favorite and most versatile building block. With this possibility in mind, we have developed a new approach, Metal Directed Protein Self-Assembly (MDPSA), which utilizes the strength, directionality and selectivity of metal-ligand interactions to control PPIs. At its core, MDPSA is inspired by supramolecular coordination chemistry which exploits metal coordination for the self-assembly of small molecules into discrete, more-or-less predictable higher-order structures. Proteins, however, are not exactly small molecules or simple metal ligands: they feature extensive, heterogeneous surfaces that can interact with each other and with metal ions in unpredictable ways. We will start this Account by first describing the challenges of using entire proteins as molecular building blocks. This will be followed by our work on a model protein (cytochrome cb562) to both highlight and overcome those challenges toward establishing some ground rules for MDPSA. Proteins are also Nature’s metal ligands of choice. In MDPSA, once metal ions guide proteins into forming large assemblies, they are by definition embedded within extensive interfaces formed between protein surfaces. These complex surfaces make an inorganic chemist’s life somewhat difficult, yet they also provide a wide platform to modulate the metal coordination environment through distant, non-covalent interactions – exactly as natural metalloproteins and enzymes do. We will describe our computational and experimental efforts on restructuring the non-covalent interaction network formed between proteins surrounding the interfacial metal centers. This approach of metal templating followed by the redesign of protein interfaces (Metal-Templated Interface Redesign, MeTIR) not only provides a route to engineer de novo PPIs and novel metal coordination environments, but also carries possible parallels to the evolution of metalloproteins.
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影响因子：
64.8
作者：
通讯作者：
--
DOI：
10.1073/pnas.0507267102
发表时间：
2005-10-11
影响因子：
11.1
作者：
Zhou, TQ;Hamer, DH;Kwong, PD
通讯作者：
Kwong, PD
影响因子：
64.5
作者：
Emsley, J;Knight, CG;Liddington, RC
通讯作者：
Liddington, RC
DOI：
10.1002/prot.340230413
发表时间：
1995-12-01
期刊：
PROTEINS-STRUCTURE FUNCTION AND GENETICS
影响因子：
--
作者：
Janin, J;Rodier, F
通讯作者：
Rodier, F
影响因子：
15
作者：
Radford RJ;Tezcan FA
通讯作者：
Tezcan FA