Transient Fibril Structures Facilitating Nonenzymatic Self-Replication
Transient Fibril Structures Facilitating Nonenzymatic Self-Replication
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DOI：
10.1021/nn302223v
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发表时间：
2012-09-01
期刊：
影响因子：
17.1
通讯作者：
Ashkenasy, Gonen
中科院分区：
文献类型：
--
作者：
Rubinov, Boris;Wagner, Nathaniel;Ashkenasy, Gonen
一个新兴的研究方向是开发“自合成材料”，这些超分子结构可以通过加速合成构建块和/或整个组装体来促进自身的形成。最近有人假设，这种系统的实际设计可以从控制两亲分子组装成纳米结构的能力中受益。本文描述了短两亲肽自组装成各种形式的可溶性-片结构-板、原纤维和空心纳米管的途径，以及它们作为自催化剂的活性，这些活性可以从更简单的构建块合成单体肽。对自组装和自我复制过程的详细动力学分析使我们能够提出一个完整的模型并模拟复制过程，揭示只有在溶液中稳定时间短于几个小时的特定结构（主要是原纤维）才能作为催化剂发挥活性。有趣的是，我们发现这样的过程也诱导了原纤维的繁殖，其机制非常类似于朊病毒蛋白通过传递错误折叠状态来繁殖。
An emerging new direction of research focuses on developing "self-synthesizing materials", those supramolecular structures that can promote their own formation by accelerating the synthesis of building blocks and/or an entire assembly. It was postulated recently that practical design of such systems can benefit from the ability to control the assembly of amphiphilic molecules into nanostructures. We describe here the self-assembly pathway of short amphiphilic peptides into various forms of soluble beta-sheet structures beta-plates, fibrils, and hollow nanotubes and their consequent activity as autocatalysts for the synthesis of monomeric peptides from simpler building blocks. A detailed kinetic analysis of both the self-assembly and self-replication processes allows us to suggest a full model and simulate the replication process, revealing that only specific structures, primarily fibrils that are stable within the solution for a time shorter than a few hours, can be active as catalysts. Interestingly, we have found that such a process also induces fibril reproduction, in a mechanism very similar to the propagation of prion proteins by transmission of misfolded states.