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Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
Chemical Society Reviews ( IF 46.2 ) Pub Date : 2017-05-22 00:00:00 , DOI: 10.1039/c6cs00542j
Gang Wei 1 , Zhiqiang Su , Nicholas P Reynolds , Paolo Arosio , Ian W Hamley , Ehud Gazit , Raffaele Mezzenga
Affiliation  

Self-assembled peptide and protein amyloid nanostructures have traditionally been considered only as pathological aggregates implicated in human neurodegenerative diseases. In more recent times, these nanostructures have found interesting applications as advanced materials in biomedicine, tissue engineering, renewable energy, environmental science, nanotechnology and material science, to name only a few fields. In all these applications, the final function depends on: (i) the specific mechanisms of protein aggregation, (ii) the hierarchical structure of the protein and peptide amyloids from the atomistic to mesoscopic length scales and (iii) the physical properties of the amyloids in the context of their surrounding environment (biological or artificial). In this review, we will discuss recent progress made in the field of functional and artificial amyloids and highlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the resulting amyloid structure and functionality. We also highlight current advances in the design and synthesis of amyloid-based biological and functional materials and identify new potential fields in which amyloid-based structures promise new breakthroughs.

中文翻译:

自组装肽和蛋白质淀粉样蛋白:从纳米技术的结构到定制功能

自组装肽和蛋白质淀粉样蛋白纳米结构传统上仅被认为是与人类神经退行性疾病有关的病理聚集体。近年来,这些纳米结构作为先进材料在生物医学、组织工程、可再生能源、环境科学、纳米技术和材料科学等领域得到了有趣的应用。在所有这些应用中,最终功能取决于:(i)蛋白质聚集的具体机制,(ii)蛋白质和肽淀粉样蛋白从原子到介观长度尺度的层次结构以及(iii)淀粉样蛋白的物理性质在周围环境(生物或人工)的背景下。在这篇综述中,我们将讨论功能性和人工淀粉样蛋白领域的最新进展,并强调蛋白质/肽折叠、解折叠和聚集机制之间的联系,以及由此产生的淀粉样蛋白结构和功能。我们还强调了基于淀粉样蛋白的生物和功能材料的设计和合成的当前进展,并确定了基于淀粉样蛋白的结构有望实现新突破的新的潜在领域。
更新日期:2017-05-31
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