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

Peng Zhang; Manola Moretti; Marco Allione; Yuansi Tian; Javier Ordonez-Loza; Davide Altamura; Cinzia Giannini; Bruno Torre; Gobind Das; Erqiang Li; Sigurdur T Thoroddsen; Mani Sarathy; Ida Autiero; Andrea Giugni; Francesco Gentile; N. Malara; Monica Marini; Enzo M. Di Fabrizio

doi:10.1038/s42003-020-01187-7

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

Peng Zhang, Manola Moretti, Marco Allione, Yuansi Tian, Javier Ordonez-Loza, Davide Altamura, Cinzia Giannini, Bruno Torre, Gobind Das, Erqiang Li, Sigurdur T Thoroddsen, Mani Sarathy, Ida Autiero, Andrea Giugni, Francesco Gentile, N. Malara, Monica Marini, Enzo M. Di Fabrizio

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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.

Original language	English (US)
Journal	Communications Biology
Volume	3
Issue number	1
DOIs	https://doi.org/10.1038/s42003-020-01187-7
State	Published - Aug 20 2020

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledged KAUST grant number(s): OCRF-2014-CRG, OCRF-2016-CRG
Acknowledgements: The authors acknowledge financial support from King Abdullah University of Science and Technology for OCRF-2014-CRG and OCRF-2016-CRG grants and from Piedmont Region through European Funds for Regional Development (“Food Digital Monitoring” project). And Istituto di Cristallografia—Consiglio Nazionale delle Ricerche (IC-CNR) would like to thank the funding from MIUR (Italian Ministry for Education, University and Re-search) in the “PON Ricerca e Competitività 2007–2013” Program: ReCaS (Azione I—Interventi di rafforzamento strutturale, PONa3_00052, Avviso 254/Ric) and PRISMA (Asse II—Sostegno ll’innovazione, PON04a2_A).

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10.1038/s42003-020-01187-7

https://repository.kaust.edu.sa/bitstream/10754/664752/1/s42003-020-01187-7.pdf

Cite this

Zhang, P., Moretti, M., Allione, M., Tian, Y., Ordonez-Loza, J., Altamura, D., Giannini, C., Torre, B., Das, G., Li, E., Thoroddsen, S. T., Sarathy, M., Autiero, I., Giugni, A., Gentile, F., Malara, N., Marini, M., & Di Fabrizio, E. M. (2020). A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth. Communications Biology, 3(1). https://doi.org/10.1038/s42003-020-01187-7

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

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.",

author = "Peng Zhang and Manola Moretti and Marco Allione and Yuansi Tian and Javier Ordonez-Loza and Davide Altamura and Cinzia Giannini and Bruno Torre and Gobind Das and Erqiang Li and Thoroddsen, {Sigurdur T} and Mani Sarathy and Ida Autiero and Andrea Giugni and Francesco Gentile and N. Malara and Monica Marini and {Di Fabrizio}, {Enzo M.}",

note = "KAUST Repository Item: Exported on 2020-10-01 Acknowledged KAUST grant number(s): OCRF-2014-CRG, OCRF-2016-CRG Acknowledgements: The authors acknowledge financial support from King Abdullah University of Science and Technology for OCRF-2014-CRG and OCRF-2016-CRG grants and from Piedmont Region through European Funds for Regional Development (“Food Digital Monitoring” project). And Istituto di Cristallografia—Consiglio Nazionale delle Ricerche (IC-CNR) would like to thank the funding from MIUR (Italian Ministry for Education, University and Re-search) in the “PON Ricerca e Competitivit{\`a} 2007–2013” Program: ReCaS (Azione I—Interventi di rafforzamento strutturale, PONa3_00052, Avviso 254/Ric) and PRISMA (Asse II—Sostegno ll{\textquoteright}innovazione, PON04a2_A).",

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doi = "10.1038/s42003-020-01187-7",

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Zhang, P , Moretti, M, Allione, M, Tian, Y, Ordonez-Loza, J, Altamura, D, Giannini, C, Torre, B, Das, G, Li, E, Thoroddsen, ST , Sarathy, M, Autiero, I, Giugni, A, Gentile, F, Malara, N, Marini, M & Di Fabrizio, EM 2020, 'A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth', Communications Biology, vol. 3, no. 1. https://doi.org/10.1038/s42003-020-01187-7

TY - JOUR

T1 - A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth

AU - Zhang, Peng

AU - Moretti, Manola

AU - Allione, Marco

AU - Tian, Yuansi

AU - Ordonez-Loza, Javier

AU - Altamura, Davide

AU - Giannini, Cinzia

AU - Torre, Bruno

AU - Das, Gobind

AU - Li, Erqiang

AU - Thoroddsen, Sigurdur T

AU - Sarathy, Mani

AU - Autiero, Ida

AU - Giugni, Andrea

AU - Gentile, Francesco

AU - Malara, N.

AU - Marini, Monica

AU - Di Fabrizio, Enzo M.

N1 - KAUST Repository Item: Exported on 2020-10-01 Acknowledged KAUST grant number(s): OCRF-2014-CRG, OCRF-2016-CRG Acknowledgements: The authors acknowledge financial support from King Abdullah University of Science and Technology for OCRF-2014-CRG and OCRF-2016-CRG grants and from Piedmont Region through European Funds for Regional Development (“Food Digital Monitoring” project). And Istituto di Cristallografia—Consiglio Nazionale delle Ricerche (IC-CNR) would like to thank the funding from MIUR (Italian Ministry for Education, University and Re-search) in the “PON Ricerca e Competitività 2007–2013” Program: ReCaS (Azione I—Interventi di rafforzamento strutturale, PONa3_00052, Avviso 254/Ric) and PRISMA (Asse II—Sostegno ll’innovazione, PON04a2_A).

PY - 2020/8/20

Y1 - 2020/8/20

N2 - 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.

AB - 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.

UR - http://hdl.handle.net/10754/664752

UR - http://www.nature.com/articles/s42003-020-01187-7

U2 - 10.1038/s42003-020-01187-7

DO - 10.1038/s42003-020-01187-7

M3 - Article

C2 - 32820203

SN - 2399-3642

VL - 3

JO - Communications Biology

JF - Communications Biology

IS - 1

ER -

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

Abstract

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