Chemical and Biomolecular Engineering, New York University, 6 MetroTech Center, Brooklyn, NY 11201, USA.
Chem Commun (Camb). 2018 Jun 14;54(49):6380-6383. doi: 10.1039/c8cc02724b.
Self-assembly of amyloid polypeptides (1) imparts biological effects depending on the size in over 20 amyloid diseases and (2) produces useful yet relatively untapped biomaterials. Unfortunately, our understanding of amyloid polypeptides, as related to biomedical implications and biomaterial applications, is limited by their self-assembling nature. In this study, we report the creation of a dual peptide system, where a pair of β-amyloid (Aβ) variants are not self-assembled but hetero-assembled in the presence of their assembly partners. We provide evidence that the resulting hetero-assemblies share molecular, structural and morphological similarities with typical amyloid self-assemblies formed by a single polypeptide (e.g., Aβ). We anticipate that our dual peptide system may readily be adapted for precise control of amyloid assembly, for the study of size-dependent neurotoxicity and precise fabrication of amyloid biomaterials.
淀粉样多肽的自组装（1）赋予了超过 20 种淀粉样疾病的生物学效应，（2）产生了有用但相对未开发的生物材料。不幸的是，由于其自组装的性质，我们对淀粉样多肽在生物医学意义和生物材料应用方面的理解是有限的。在这项研究中，我们报告了一种双肽系统的创建，其中一对β-淀粉样蛋白（Aβ）变体不会自组装，但在其组装伙伴的存在下会异组装。我们提供的证据表明，所得的异组装与由单个多肽（例如 Aβ）形成的典型淀粉样自组装具有分子、结构和形态上的相似性。我们预计，我们的双肽系统可以很容易地适应于精确控制淀粉样蛋白的组装，用于研究尺寸依赖性神经毒性和精确制造淀粉样生物材料。
