Super-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.

Confined laminar flow on a super-hydrophobic surface drives the initial stages of tau protein aggregation / M. Moretti, M. Allione, M. Marini, A. Giugni, B. Torre, G. Das, E. Di Fabrizio. - In: MICROELECTRONIC ENGINEERING. - ISSN 0167-9317. - 191(2018 May 05), pp. 54-59. [10.1016/j.mee.2018.01.025]

Confined laminar flow on a super-hydrophobic surface drives the initial stages of tau protein aggregation

A. Giugni;
2018

Abstract

Super-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.
Amyloid β-sheet; Confined laminar flow; Raman spectroscopy; Super-hydrophobic device; Tau protein
Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin)
1-feb-2018
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/825619
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