The authors describe the interaction of biological nanostructures formed by beta 2-microglobulin amyloid fibrils with three-dimensional silicon microstructures consisting in periodic arrays of vertical silicon walls (3 mu m-thick) separated by 50 mu m-deep air gaps (5 mu m-wide). These structures are of great interest from a biological point of view since they well mimic the interstitial environment typical of amyloid deposition in vivo. Moreover, they behave as hybrid photonic crystals, potentially applicable as optical transducers for label-free detection of the kinetics of amyloid fibrils formation. Fluorescence and atomic force microscopy (AFM) show that a uniform distribution of amyloid fibrils is achieved when fibrillogenesis occurs directly on silicon. The high resolution AFM images also demonstrate that amyloid fibrils grown on silicon are characterized by the same fine structure typically ensured by fibrillogenesis in solution.

Fibrillogenesis of human beta2-microglobulin in three-dimensional silicon microstructures

MERLO, SABINA GIOVANNA;CARPIGNANO, FRANCESCA MARIA CARLA;SILVA, GLORIA;GIORGETTI, SOFIA;STOPPINI, MONICA;BELLOTTI, VITTORIO
2012-01-01

Abstract

The authors describe the interaction of biological nanostructures formed by beta 2-microglobulin amyloid fibrils with three-dimensional silicon microstructures consisting in periodic arrays of vertical silicon walls (3 mu m-thick) separated by 50 mu m-deep air gaps (5 mu m-wide). These structures are of great interest from a biological point of view since they well mimic the interstitial environment typical of amyloid deposition in vivo. Moreover, they behave as hybrid photonic crystals, potentially applicable as optical transducers for label-free detection of the kinetics of amyloid fibrils formation. Fluorescence and atomic force microscopy (AFM) show that a uniform distribution of amyloid fibrils is achieved when fibrillogenesis occurs directly on silicon. The high resolution AFM images also demonstrate that amyloid fibrils grown on silicon are characterized by the same fine structure typically ensured by fibrillogenesis in solution.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11571/353727
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