A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth
| العنوان: | A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth |
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| المؤلفون: | Cinzia Giannini, Manola Moretti, Bruno Torre, Davide Altamura, Yuansi Tian, Erqiang Li, Enzo Di Fabrizio, Natalia Malara, Javier Ordonez-Loza, Andrea Giugni, Peng Zhang, Francesco Gentile, Marco Allione, S. Mani Sarathy, Ida Autiero, Sigurdur T. Thoroddsen, Gobind Das, Monica Marini |
| المصدر: | Communications Biology Communications Biology, Vol 3, Iss 1, Pp 1-13 (2020) |
| بيانات النشر: | Nature Publishing Group UK, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | Amyloid, Protein Folding, Materials science, Convective flow, Future studies, Medicine (miscellaneous), Peptide, 02 engineering and technology, macromolecular substances, Molecular Dynamics Simulation, Fibril, Microscopy, Atomic Force, complex mixtures, Spectrum Analysis, Structure-Activity Relationship, X-Ray Diffraction, Hydrophobic and Hydrophilic Interactions, Protein Aggregates, General Biochemistry, Genetics and Molecular Biology, Article, 03 medical and health sciences, Molecular dynamics, symbols.namesake, Microscopy, Biopolymers in vivo, lcsh:QH301-705.5, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Lab-on-a-chip, technology, industry, and agriculture, Atomic Force, 021001 nanoscience & nanotechnology, Amyloid fibril, lcsh:Biology (General), chemistry, Raman spectroscopy, Biophysics, symbols, 0210 nano-technology, General Agricultural and Biological Sciences |
| الوصف: | 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. Zhang et al present an integrated real-time imaging and flow field control platform based on water droplet evaporation on super-hydrophobic substrate (SHS) to enable amyloid fibril aggregation. They apply this methodology to observe structural polymorphism in PHF6 peptide and full length Tau441. |
| اللغة: | English |
| تدمد: | 2399-3642 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d930d67d2ccbb7181391c24d8ff62ebd http://europepmc.org/articles/PMC7441408 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....d930d67d2ccbb7181391c24d8ff62ebd |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 23993642 |
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