Recent advances in nanofibrous assemblies based on β-sheet-forming peptides for biomedical applications

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• 作者：Tomonori Waku and Naoki Tanaka
• 刊名：Polymer International
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：66
• 期：2
• 页码：277-288
• 全文大小：1642K
• ISSN：1097-0126

文摘

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.