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

1 Scopus citations

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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