期刊
COMMUNICATIONS BIOLOGY
卷 3, 期 1, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s42003-020-01187-7
关键词
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资金
- King Abdullah University of Science and Technology [OCRF-2014-CRG, OCRF-2016-CRG]
- Piedmont Region through European Funds for Regional Development (Food Digital Monitoring project)
- MIUR (Italian Ministry for Education, University and Re-search) in the PON Ricerca e Competitivita 2007-2013 Program: ReCaS (Azione I-Interventi di rafforzamento strutturale) [PONa3_00052, Avviso 254/Ric]
- MIUR (Italian Ministry for Education, University and Re-search) in the PON Ricerca e Competitivita 2007-2013 Program: PRISMA (Asse II-Sostegno ll'innovazione) [PON04a2_A]
Methods to produce protein amyloid fibrils, in vitro, and in situ structure characterization, are of primary importance in biology, medicine, and pharmacology. We first demonstrated the droplet on a super-hydrophobic substrate as the reactor to produce protein amyloid fibrils with real-time monitoring of the growth process by using combined light-sheet microscopy and thermal imaging. The molecular structures were characterized by Raman spectroscopy, X-ray diffraction and X-ray scattering. We demonstrated that the convective flow induced by the temperature gradient of the sample is the main driving force in the growth of well-ordered protein fibrils. Particular attention was devoted to PHF6 peptide and full-length Tau441 protein to form amyloid fibrils. By a combined experimental with the molecular dynamics simulations, the conformational polymorphism of these amyloid fibrils were characterized. The study provided a feasible procedure to optimize the amyloid fibrils formation and characterizations of other types of proteins in future studies. Zhang et al present an integrated real-time imaging and flow field control platform based on water droplet evaporation on super-hydrophobic substrate (SHS) to enable amyloid fibril aggregation. They apply this methodology to observe structural polymorphism in PHF6 peptide and full length Tau441.
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