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.

A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth / P. Zhang, M. Moretti, M. Allione, Y. Tian, J. Ordonez-Loza, D. Altamura, C. Giannini, B. Torre, G. Das, E. Li, S.T. Thoroddsen, S.M. Sarathy, I. Autiero, A. Giugni, F. Gentile, N. Malara, M. Marini, E. Di Fabrizio. - In: COMMUNICATIONS BIOLOGY. - ISSN 2399-3642. - 3:1(2020 Aug 20), pp. 457.1-457.13. [10.1038/s42003-020-01187-7]

A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth

A. Giugni;
2020

Abstract

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.
Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/823923
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