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Amyloid Fibrils: Nanoscale Heterogeneity of the Molecular Structure of Individual hIAPP Amyloid Fibrils Revealed with Tip‐Enhanced Raman Spectroscopy (Small 33/2015)
Author(s) -
vandenAkker Corianne C.,
DeckertGaudig Tanja,
Schleeger Michael,
Velikov Krassimir P.,
Deckert Volker,
Bonn Mischa,
Koenderink Gijsje H.
Publication year - 2015
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201570202
Subject(s) - fibril , amyloid (mycology) , chemistry , raman spectroscopy , amyloid fibril , biophysics , nanoscopic scale , surface enhanced raman spectroscopy , nanotechnology , materials science , amyloid β , biochemistry , raman scattering , biology , optics , medicine , inorganic chemistry , physics , disease , pathology
Many diseases, including type 2 diabetes, are linked to the pathological deposition of nanoscale, fibrillar protein aggregates called amyloids. Since the surface of amyloid fibrils plays a key role in amyloid toxicity and membrane damage, knowledge of the surface structure is essential. On page 4131, V. Deckert, G. H. Koenderink, and co‐workers probe the molecular structure and amino acid residue composition with tipenhanced Raman spectroscopy. The surface of amyloid fibrils contains mainly unstructured or α‐helical structures, in contrast to the core, which is dominated by β‐sheets.