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Peptide Amyloids in the Origin of Life

机译：肽淀粉样蛋白在生命起源

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How life can emerge from non-living matter is one of the fundamental mysteries of the universe. A bottom-up approach to this problem focuses on the potential chemical precursors of life, in particular the nature of the first replicative molecules. Such thinking has led to the currently most popular idea: that an RNA-like molecule played a central role as the first replicative and catalytic molecule. Here, we review an alternative hypothesis that has recently gained experimental support, focusing on the role of amyloidogenic peptides rather than nucleic acids, in what has been by some termed "the amyloid-world" hypothesis. Amyloids are well-ordered peptide aggregates that have a fibrillar morphology due to their underlying structure of a one-dimensional crystal-like array of peptides in a beta-strand conformation. While they are notorious for their implication in several neurodegenerative diseases including Alzheimer's disease, amyloids also have many biological functions. In this review, we will elaborate on the following properties of amyloids in relation to their fitness as a prebiotic entity: they can be formed by very short peptides with simple amino acids sequences; as aggregates they are more chemically stable than their isolated component peptides; they can possess diverse catalytic activities; they can form spontaneously during the prebiotic condensation of amino acids; they can act as templates in their own chemical replication; they have a structurally repetitive nature that enables them to interact with other structurally repetitive biopolymers like RNA/DNA and polysaccharides, as well as with structurally repetitive surfaces like amphiphilic membranes and minerals. (C) 2018 Elsevier Ltd. All rights reserved.
机译：生活如何从非生物中出现是宇宙的基本奥秘之一。这个问题的自下而上的方法侧重于潜在的生命中的化学前体，特别是第一复制分子的性质。这种思想导致了目前最受欢迎的想法：类似RNA样子作为第一复制和催化分子起到了中心作用。在这里，我们审查了最近获得了实验支持的替代假设，重点是淀粉样蛋白肽而不是核酸的作用，在一些称为“淀粉样蛋白世界”假设中是什么。淀粉样蛋白是由于其在β-链构象中的一维晶状串的底层结构而具有纤维状形态的良好有序的肽聚集体。虽然它们在包括阿尔茨海默病等几种神经变性疾病中的暗示中令人震惊，但淀粉样蛋白也具有许多生物学功能。在本综述中，我们将详细阐述与益生元实体相比的淀粉样蛋白的性质：它们可以通过具有简单氨基酸序列的非常短的肽形成;作为聚集体，它们比其分离的组分肽更具化学稳定;他们可以拥有多种催化活动;它们可以在氨基酸益生菌凝结期间自发形成;他们可以在自己的化学复制中作为模板;它们具有结构重复性质，使它们能够与其他结构重复的生物聚合物相互作用，如RNA / DNA和多糖，以及与两亲膜和矿物质等结构重复的表面相互作用。 （c）2018年elestvier有限公司保留所有权利。

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