Raman study of lysozyme amyloid fibrils suspended on super-hydrophobic surfaces by shear flow
Di Fabrizio, Enzo M.
KAUST DepartmentPhysical Sciences and Engineering (PSE) Division
Biological and Environmental Sciences and Engineering (BESE) Division
Permanent link to this recordhttp://hdl.handle.net/10754/623703
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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.
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.
SponsorsThe 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.