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dc.contributor.authorMoretti, Manola
dc.contributor.authorAllione, Marco
dc.contributor.authorMarini, Monica
dc.contributor.authorGiugni, Andrea
dc.contributor.authorTorre, Bruno
dc.contributor.authorDas, Gobind
dc.contributor.authorDi Fabrizio, Enzo M.
dc.date.accessioned2018-02-07T07:02:24Z
dc.date.available2018-02-07T07:02:24Z
dc.date.issued2018-02-01
dc.identifier.citationMoretti M, Allione M, Marini M, Giugni A, Torre B, et al. (2018) Confined laminar flow on a super-hydrophobic surface drives the initial stages of tau protein aggregation. Microelectronic Engineering 191: 54–59. Available: http://dx.doi.org/10.1016/j.mee.2018.01.025.
dc.identifier.issn0167-9317
dc.identifier.doi10.1016/j.mee.2018.01.025
dc.identifier.urihttp://hdl.handle.net/10754/627051
dc.description.abstractSuper-hydrophobic micro-patterned surfaces are ideal substrates for the controlled self-assembly and substrate-free characterization of biological molecules. In this device, the tailored surface supports a micro-volume drop containing the molecules of interest. While the quasi-spherical drop is evaporating under controlled conditions, its de-wetting direction is guided by the pillared microstructure on top of the device, leading to the formation of threads between the neighboring pillars. This effect has been exploited here to elucidate the mechanism triggering the formation of amyloid fibers and oligomers in tau related neurodegenerative diseases. By using Raman spectroscopy, we demonstrate that the fiber bridging the pillars contains β-sheets, a characteristic feature of amyloid aggregation. We propose that the combination of laminar flow, shear stress and molecular crowding taking place while the drop is evaporating on the SHMS, induces the reorganization of the tau protein secondary structure and we suggest that this effect could in fact closely mimic the actual mechanism occurring in the human brain environment. Such a straightforward technique opens up new possibilities in the field of self-assembly of biomolecules and their characterization by different methods (SEM, AFM, Raman spectroscopy, TEM), in a single device.
dc.description.sponsorshipThe authors acknowledge financial support from King Abdullah University of Science and Technology for OCRF-2014-CRG and OCRF-2016-CRG grants, the Italian Ministry of Health under project nos. GR-2010-2320665 and GR-2010-2311677.
dc.publisherElsevier BV
dc.relation.urlhttp://www.sciencedirect.com/science/article/pii/S016793171830042X
dc.rightsNOTICE: this is the author’s version of a work that was accepted for publication in Microelectronic Engineering. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Microelectronic Engineering, [, , (2018-02-01)] DOI: 10.1016/j.mee.2018.01.025 . © 2018. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectSuper-hydrophobic device
dc.subjectAmyloid β-sheet
dc.subjectTau protein
dc.subjectRaman spectroscopy
dc.subjectConfined laminar flow
dc.titleConfined laminar flow on a super-hydrophobic surface drives the initial stages of tau protein aggregation
dc.typeArticle
dc.contributor.departmentMaterial Science and Engineering Program
dc.contributor.departmentPhysical Science and Engineering (PSE) Division
dc.identifier.journalMicroelectronic Engineering
dc.eprint.versionPost-print
kaust.personMoretti, Manola
kaust.personAllione, Marco
kaust.personMarini, Monica
kaust.personGiugni, Andrea
kaust.personTorre, Bruno
kaust.personDas, Gobind
kaust.personDi Fabrizio, Enzo M.
kaust.grant.numberOCRF-2014-CRG
kaust.grant.numberOCRF-2016-CRG
refterms.dateFOA2020-02-01T00:00:00Z
dc.date.published-online2018-02-01
dc.date.published-print2018-05


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