ABSTRACT

Fluorinated nanoparticles induce α-helix rich structures in amyloid β-peptide at pH 7 whereas the alkylated ones lead to β-sheet formation. Fluorinated nanoparticles are proposed to be potential candidates for the inhibition and reversion of conformational changes of proteins that lead to amyloid fibril formation. Amyloid β-peptide is found in cerebrovascular deposits and extracellular neuritic plaques that characterize Alzheimer’s disease, a progressive neurodegenerative disorder of the human brain. The fact that mutations in the amyloid protein precursor gene are associated with Alzheimer’s disease is a strong indication of the importance of amyloid in the pathogenesis of the disease. The delineation of the amyloid β-peptide hypothesis predicts therapeutics based on preventing the peptide misfolding and aggregation.