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dc.contributor.authorMoretti, Manola
dc.contributor.authorAllione, Marco
dc.contributor.authorMarini, Monica
dc.contributor.authorTorre, Bruno
dc.contributor.authorGiugni, Andrea
dc.contributor.authorLimongi, Tania
dc.contributor.authorDas, Gobind
dc.contributor.authorDi Fabrizio, Enzo M.
dc.date.accessioned2017-05-23T09:30:36Z
dc.date.available2017-05-23T09:30:36Z
dc.date.issued2017-05-19
dc.identifier.citationMoretti M, Allione M, Marini M, Torre B, Giugni A, et al. (2017) Raman study of lysozyme amyloid fibrils suspended on super-hydrophobic surfaces by shear flow. Microelectronic Engineering 178: 194–198. Available: http://dx.doi.org/10.1016/j.mee.2017.05.045.
dc.identifier.issn0167-9317
dc.identifier.doi10.1016/j.mee.2017.05.045
dc.identifier.urihttp://hdl.handle.net/10754/623703
dc.description.abstractThe shear flow generated at the rim of a drop evaporating on a micro-fabricated super-hydrophobic surface has been used to suspend and orient single/few lysozyme amyloid fibrils between two pillars for substrate-free characterization. Micro Raman spectroscopy performed on extended fibers evidenced a shift of the Amide I band main peak to the value attributed to β-sheet secondary structure, characteristic of the amyloid fibers. In addition, given the orientation sensitivity of the anisotropic molecule, the Raman signal of the main secondary structure was nicely enhanced for a fiber alignment parallel to the polarization direction of the laser. The substrate-free sample generated by this suspending technique is suitable for other structural analysis methods, where fiber crystals are investigated. It could be further employed for generation of arrays and patterns in a controllable fashion, where bio-compatible material is needed.
dc.description.sponsorshipThe authors acknowledge financial support from the KAUST start-up funding and from Ministry of Health, Italy under the projects: Project no.: GR-2010-2320665 and Project no.: GR-2010-2311677.
dc.publisherElsevier BV
dc.relation.urlhttp://www.sciencedirect.com/science/article/pii/S0167931717302423
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, [, , (2017-05-19)] DOI: 10.1016/j.mee.2017.05.045 . © 2017. 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 micro-patterned surfaces
dc.subjectRaman spectroscopy
dc.subjectAmyloid fibrils
dc.subjectβ-sheet secondary structure
dc.titleRaman study of lysozyme amyloid fibrils suspended on super-hydrophobic surfaces by shear flow
dc.typeArticle
dc.contributor.departmentPhysical Sciences and Engineering (PSE) Division
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.identifier.journalMicroelectronic Engineering
dc.eprint.versionPost-print
dc.contributor.institutionBio-Nanotechnology and Engineering for Medicine (BIONEM), Department of Experimental and Clinical Medicine, University of Magna Graecia Viale Europa, Germaneto, Catanzaro 88100, Italy
kaust.personMoretti, Manola
kaust.personAllione, Marco
kaust.personMarini, Monica
kaust.personTorre, Bruno
kaust.personGiugni, Andrea
kaust.personLimongi, Tania
kaust.personDas, Gobind
kaust.personDi Fabrizio, Enzo M.


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