Institute of Experimental Physics
Topic
Protein stability and aggregation in biocompatible organic solvents
PhD. program
Biophysics
Name of the supervisor
RNDr. Diana Fedunová, PhD.
Contact:
Receiving school
Faculty of Science, P.J. Safarik University
Annotation
The identification of effective solvents capable of modulating protein stability and aggregation is of great importance for various applications in biotechnology or medicine. The production and long-term storage of proteins requires setting appropriate environmental conditions that preserve the native structure of the proteins and prevent their aggregation. Similarly, the formation of a special type of ordered aggregates - amyloid fibrils, is modulated by external conditions. Amyloid aggregates represent new potential biomaterials due to their unique properties. Therefore, finding conditions capable of inducing the formation of defined amyloid aggregates is of interest. This work aims to study the effect of special solvents - ionic liquids and deep eutectic mixtures – on the stability, kinetics of amyloid aggregation, and morphology of amyloid fibrils of various proteins (lysozyme, insulin). The objective is to determine the relationship between solvent’s composition and physicochemical properties and their ability to stabilize/destabilize protein structure and inhibit/accelerate amyloid aggregation to find solvents capable of stabilizing studied proteins or inducing amyloid aggregate formation with defined morphology. Spectroscopic (UV-VIS, CD, FTIR) and calorimetric (DSC, ITC) methods, as well as atomic force microscopy (AFM) and computer image analysis methods, will be used.