TY - JOUR
T1 - Self-assembling peptide and protein amyloids
T2 - From structure to tailored function in nanotechnology
AU - Wei, Gang
AU - Su, Zhiqiang
AU - Reynolds, Nicholas P.
AU - Arosio, Paolo
AU - Hamley, Ian W.
AU - Gazit, Ehud
AU - Mezzenga, Raffaele
N1 - Publisher Copyright:
© 2017 The Royal Society of Chemistry.
PY - 2017/8/7
Y1 - 2017/8/7
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85026662703&partnerID=8YFLogxK
U2 - 10.1039/c6cs00542j
DO - 10.1039/c6cs00542j
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C2 - 28530745
AN - SCOPUS:85026662703
SN - 0306-0012
VL - 46
SP - 4661
EP - 4708
JO - Chemical Society Reviews
JF - Chemical Society Reviews
IS - 15
ER -