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Fibrillogenesis of human β 2 ‐microglobulin in three‐dimensional silicon microstructures
Author(s) -
Merlo Sabina,
Barillaro Giuseppe,
Carpignano Francesca,
Silva Gloria,
Surdo Salvatore,
Strambini Lucanos M.,
Giorgetti Sofia,
Nichino Daniela,
Relini Annalisa,
Mazzini Giuliano,
Stoppini Monica,
Bellotti Vittorio
Publication year - 2012
Publication title -
journal of biophotonics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.877
H-Index - 66
eISSN - 1864-0648
pISSN - 1864-063X
DOI - 10.1002/jbio.201100132
Subject(s) - fibrillogenesis , silicon , fibril , amyloid fibril , amyloid (mycology) , chemistry , materials science , nanotechnology , beta 2 microglobulin , nanostructure , biophysics , optoelectronics , amyloid β , medicine , inorganic chemistry , biochemistry , disease , pathology , biology
The authors describe the interaction of biological nanostructures formed by β 2 ‐microglobulin amyloid fibrils with three‐dimensional silicon microstructures consisting in periodic arrays of vertical silicon walls (≈3 μm‐thick) separated by 50 μm‐deep air gaps (≈5 μm‐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. (© 2012 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)