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Adsorption of Amyloid β‐Peptide at Polymer Surfaces: A Neutron Reflectivity Study
Author(s) -
Rocha Sandra,
Krastev Rumen,
Thünemann Andreas F.,
Pereira M. Carmo,
Möhwald Helmuth,
Brezesinski Gerald
Publication year - 2005
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200500158
Subject(s) - peptide , adsorption , neutron reflectometry , chemistry , sulfonate , chemical engineering , aqueous solution , polystyrene , amyloid (mycology) , hydrophobic effect , allylamine , polymer , polymer chemistry , polyelectrolyte , organic chemistry , inorganic chemistry , sodium , neutron , neutron scattering , small angle neutron scattering , biochemistry , physics , quantum mechanics , engineering
Abstract The adsorption of amyloid β ‐peptide at hydrophilic and hydrophobic modified silicon–liquid interfaces was characterized by neutron reflectometry. Distinct polymeric films were used to obtain noncharged (Formvar), negatively (sodium poly(styrene sulfonate)) and positively charged (poly(allylamine hydrochloride)) hydrophilic as well as hydrophobic surfaces (polystyrene and a polysiloxane–dodecanoic acid complex). Amyloid β ‐peptide was found to adsorb at positively charged hydrophilic and hydrophobic surfaces, whereas no adsorbed layer was detected on hydrophilic noncharged and negatively charged films. The peptide adsorbed at the positively charged film as patches, which were dispersed on the surface, whereas a uniform layer was observed at hydrophobic surfaces. The thickness of the adsorbed peptide layer was estimated to be approximately 20 Å. The peptide formed a tightly packed layer, which did not contain water. These studies provide information about the affinity of the amyloid β ‐peptide to different substrates in aqueous solution and suggest that the amyloid fibril formation may be driven by interactions with surfaces.