Recent advances in nanofibrous assemblies based on β‐sheet‐forming peptides for biomedical applications
Recent advances in nanofibrous assemblies based on β‐sheet‐forming peptides for biomedical applications
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DOI：
10.1002/pi.5195
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发表时间：
2017-02
影响因子：
3.2
通讯作者：
Tomonori Waku;N. Tanaka
中科院分区：
文献类型：
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作者：
Tomonori Waku;N. Tanaka
淀粉样原纤维是由蛋白质/肽通过分子间相互作用聚合而形成的具有富含β-片层结构的超分子聚合物。淀粉样原纤维一直被误认为是有毒的恶棍，因为它们历来被研究为与阿尔茨海默氏症和帕金森氏症等严重疾病相关的病原体。然而，最近对其毒性和形成机制的研究以及其在自然界中功能的发现纠正了这一误解，并有力地促进了β-折叠形成肽在设计新型纳米材料中的可能用途。在一定条件下，基于β-折叠形成肽的自组装可以提供高度有序的纳米结构。因此，巧妙设计的积木肽允许构建纳米组装体，其包含大量的生物功能分子，包括药物和生物活性肽，并表现出独特的性质，例如响应外部刺激或特定分子的组装或拆卸。这些特性为创造创新的纳米材料提供了一种新的策略，特别是用于生物医学应用。本文综述了基于β-折叠肽的纤维组装体在生物医学领域的应用，如抑制蛋白质聚集、控制释放、组织工程等方面的研究进展。本文不仅对纳米纤维组装体的功能进行了综述，还对组成分子淀粉样蛋白生成肽的功能进行了综述。中国化学工业协会
Amyloid fibrils are supramolecular polymers with β-sheet-rich structures formed by polymerization of protein/peptide with intermolecular interaction. Amyloid fibrils have been miscast as toxic villains since they have historically been studied as pathogens associated with serious diseases, including Alzheimer's and Parkinson's disease. However, recent studies on their toxicity and formation mechanism and discovery of their functionality in nature correct the misconception and strongly facilitate the possible use of β-sheet-forming peptides in designing novel nanomaterials. Self-assembly based on β-sheet-forming peptides can provide highly ordered nanostructures under certain conditions. Therefore, ingenious design of the building block peptides allows the construction of nano-assemblies, which contain large quantities of bio-functional molecules, including drugs and bioactive peptides, and exhibit unique properties, such as assembly or disassembly in response to external stimulus or specific molecules. These properties provide a novel strategy for the creation of innovative nanomaterials, especially for biomedical applications. Here, we describe recent progress in the biomedical application of fibrous assemblies based on β-sheet-forming peptides, such as the suppression of aberrant protein aggregation, controlled release, tissue engineering and other applications. This review focuses not only on the function of the nanofibrous assemblies but also on the functions of component molecules, namely amyloidogenic peptides. © 2016 Society of Chemical Industry