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       The aim of the project is the study of time- and pH-dependent conformational changes of β-amyloid peptides in the presence of metal ions and antiamyloid compounds (resveratrol, clioquinol, curcumin, NOSH-aspirins, NAP-like peptides) or aggregation factors like Aβ(25-35) peptide, which will allow a better understanding of their involvement in the neurodegenerative diseases. Techniques like mass spectrometry at various pH values, solid phase peptide synthesis, circular dichroism, infrared, nuclear magnetic resonance and fluorescence spectroscopy, or atomic force microscopy will show how metal-Aβ coordination promotes aggregation. Here we probe the structures and mechanisms through which metal ions can affect amyloidosis, and the role of small changes of pH on time-dependent metal binding to peptides. In vitro formation and degradation of β-amyloid aggregates and fibrils under various conditions of pH, concentration of metal ions or aggregation and antiaggregating agents will be investigated. Findings will be published in high ranked journals.



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