A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth(429 views) Zhang P, Moretti M, Allione M, Tian Y, Ordonez-loza J, Altamura D, Giannini C, Torre B, Das G, Li E, Thoroddsen ST, Sarathy SM, Autiero I, Giugni A, Gentile F, Malara N, Marini M, Di Fabrizio E
Commun Biol (ISSN: 2399-3642linking), 2020 Aug 20; 3(1): 457-457.
Paper type: Journal Article, Research Support, Non-U. S. Gov'T
Impact factor: 12.121, 5-year impact factor: 0
Url: Not available.
Keywords: Amyloid Chemistry Ultrastructure
, Hydrophobic And Hydrophilic Interactions
, Microscopy, Atomic Force
, Molecular Dynamics Simulation
, Protein Aggregates
, Protein Folding
, Spectrum Analysis
, Structure-Activity Relationship
, X-Ray Diffraction
Affiliations: *** IBB - CNR ***
SMILEs Lab, Physical Science and Engineering (PSE) and Biological and Environmental Science and Engineering (BESE) Divisions, King Abdullah University of Science and Technology, Thuwal, 23955-6900, Saudi Arabia.
High-Speed Fluids Imaging Lab, Physical Science and Engineering (PSE) Division, King Abdullah University of Science and Technology, Thuwal, 23955-6900, Saudi Arabia.
Clean Combustion Research Center, Physical Science and Engineering (PSE) Division, King Abdullah University of Science and Technology, Thuwal, 23955-6900, Saudi Arabia.
Istituto di Cristallografia - Consiglio Nazionale delle Ricerche (IC-CNR), Via Amendola 122/O, 70126, Bari, Italy.
Department of Physics, Khalifa University, P.O. Box: 127788, Abu Dhabi, UAE.
Department of Modern Mechanics, University of Science and Technology of China, Hefei, Anhui, 230026, China.
Molecular Horizon, Bettona, Italy.
National Research Council, Institute of Biostructures and Bioimaging, Naples, Italy.
Department of electrical Engineering and Information Technology, University Federico II, Naples, Italy.
BIONEM lab, University Magna Graecia, Campus Salvatore Venuta, Viale Europa, 88100, Catanzaro, Italy.
Materials and Microsystems Laboratory, Department of Applied Science and Technology, Politecnico di Torino, 10129, Torino, Italy.
References: Not available.
A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth
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