Wei Gang, Su Zhiqiang, Reynolds Nicholas P, Arosio Paolo, Hamley Ian W, Gazit Ehud, Mezzenga Raffaele
Faculty of Production Engineering, University of Bremen, Bremen, Germany.
Chem Soc Rev. 2017 Jul 31;46(15):4661-4708. doi: 10.1039/c6cs00542j.
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.
自组装肽和蛋白质淀粉样纳米结构传统上仅被视为与人类神经退行性疾病相关的病理聚集体。近年来,这些纳米结构在生物医学、组织工程、可再生能源、环境科学、纳米技术和材料科学等先进材料领域有了有趣的应用,仅举几个领域为例。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)从原子尺度到介观尺度的蛋白质和肽淀粉样蛋白的层次结构,以及(iii)淀粉样蛋白在其周围环境(生物或人工)背景下的物理性质。在本综述中,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、解折叠和聚集机制与所得淀粉样结构和功能之间的联系。我们还强调了基于淀粉样蛋白的生物和功能材料设计与合成的当前进展,并确定了基于淀粉样蛋白的结构有望取得新突破的新潜在领域。