Main objective: 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.

The specific objective is to study the time- and pH-dependent formation and complex interactions of amyloid peptides with both aggregating and anti-aggregating agents using our patented high pH mass spectrometric (MS) and other modern techniques (NMR, CD, FTIR, AFM, SEM, DLS etc), under various concentration & solvent conditions (outcome: a new patent, three highly ranked papers, invited talks at international meetings). Another project objective is to prove the effectiveness of mass spectrometric measurements and to confirm the formation or dissolution of amyloid complexes at various pH values by other instrumental techniques than MS, such as infrared, fluorescence or UV-vis spectroscopy, atomic force microscopy, scanning electron microscopy, dynamic light scattering etc (Project outcome: international conferences, papers, improved MS techniques). Our research will increase understanding of the pathways involved in protein aggregation, and to highlight the possible molecular mechanisms of cellular toxicity (outcome: published papers in Biomacromolecules, J. Neurochem., Curr. Alzheimer Res. or Alzheimer Res. Ther). These may lead to approaches toward rational therapeutics. Besides, PhD students will be integrated in the project and trained with the instruments, reagent and protocols usage. They will write their theses, make oral and poster presentations, and will become co-authors of papers and patents (another project outcome).