Institute of Experimental Physics
The effect of various interaction partners on protein amyloid aggregation
Name of the supervisor
doc. RNDr. Zuzana Gažová, CSc.
Faculty of Science P.J. Safarik University
Amyloidoses represent a group of more than 50 so far incurable diseases, the pathological manifestation of which is the presence of deposits containing protein amyloid fibrils in tissues and organs. The formation of amyloid aggregates is due to transformation of native protein conformation into non-native conformers following their polymerization into amyloid fibrils. The main goal of the thesis is to study of the formation and morphology of Aβ peptide, insulin and lysozyme amyloid fibrils associated with Alzheimer's disease, diabetes mellitus or lysozyme amyloidosis. We will observe how various agents (ions, small molecules, nanoparticles, poly / peptides) influence the formation of amyloid fibrils of the above-mentioned proteins in order to find potential drugs for amyloid diseases. Various biophysical methods will be used, especially spectroscopic and calorimetric techniques, atomic force microscopy (AFM) and electrophoretic techniques.