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.
Original language | English (US) |
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Pages (from-to) | 54-59 |
Number of pages | 6 |
Journal | Microelectronic Engineering |
Volume | 191 |
DOIs | |
State | Published - May 5 2018 |
Bibliographical note
Publisher Copyright:© 2018 Elsevier B.V.
Keywords
- Amyloid β-sheet
- Confined laminar flow
- Raman spectroscopy
- Super-hydrophobic device
- Tau protein
ASJC Scopus subject areas
- Electronic, Optical and Magnetic Materials
- Atomic and Molecular Physics, and Optics
- Condensed Matter Physics
- Surfaces, Coatings and Films
- Electrical and Electronic Engineering