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

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
JournalCommunications Biology
Volume3
Issue number1
DOIs
StatePublished - Aug 20 2020

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