TY - JOUR A1 - Rocha, S. A1 - Thünemann, Andreas A1 - do Carmo Pereira, M. A1 - Coelho, M. A1 - Möhwald, H. A1 - Brezesinski, G. T1 - Influence of fluorinated and hydrogenated nanoparticles on the structure and fibrillogenesis of amyloid beta-peptide JF - Biophysical chemistry N2 - Peptide aggregation in amyloid fibrils is implicated in the pathogenesis of several diseases such as Alzheimer's disease. There is a strong correlation between amyloid fibril formation and a decrease in conformational stability of the native state. Amyloid-β peptide (Aβ), the aggregating peptide in Alzheimer's disease, is natively unfolded. The deposits found in Alzheimer's disease are composed of Aβ fibrillar aggregates rich in β-sheet structure. The influence of fluorinated complexes on the secondary structure and fibrillogenesis of Aβ peptide was studied by circular dichroism (CD) spectroscopy and transmission electron microscopy (TEM). CD spectra show that complexes of polyampholyte and fluorinated dodecanoic acid induce a-helix structure in Aβ, but their hydrogenated analogous lead to β-sheet formation and aggregation. The fluorinated nanoparticles with highly negative zeta potential and hydrophobic fluorinated core have the fundamental characteristics to prevent Aβ fibrillogenesis. KW - Amyloid beta-peptide KW - Circular dichroism KW - Conformation analysis KW - Electron microscopy KW - Fluorinated complexes KW - Nanoparticles PY - 2008 DO - https://doi.org/10.1016/j.bpc.2008.06.010 SN - 0301-4622 SN - 1873-4200 VL - 137 IS - 1 SP - 35 EP - 42 PB - Elsevier CY - Amsterdam AN - OPUS4-17810 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER -