Institute of Experimental Physics
Topic
Amyloid Fibrils of α-Lactalbumin and Lysozyme: Formation, Characterization, and Stability in Complex Systems
PhD. program
Biophysics
Year of admission
2026
Name of the supervisor
RNDr. Andrea Antošová, PhD.
Contact:
Receiving school
Faculty of Science, P.J. Safarik University
Annotation
Amyloid aggregation is a process by which native proteins undergo a structural transformation into highly ordered amyloid fibrils with a characteristic cross-β sheet secondary structure. Although amyloid fibrils have traditionally been associated with pathological conditions known as amyloidoses, recent research highlights their potential applications in biotechnology and the food industry, particularly as bioactive proteins with added nutritional value. α-Lactalbumin (α-LA) and lysozyme are well-characterized globular proteins that naturally occur in food matrices. α-Lactalbumin, a protein present in mammalian milk, and lysozyme, an enzyme found primarily in egg white and mammalian secretions, represent suitable model systems for studying the formation of amyloid fibrils and hydrogels. Lysozyme is known for its high stability, antimicrobial activity, and ability to form amyloid fibrils under defined denaturing conditions, making it an attractive model for investigating the relationship between structure, stability, and functional properties of amyloid systems. The aim of this doctoral thesis is to identify and optimize conditions leading to the formation of amyloid fibrils and hydrogels of α-lactalbumin and lysozyme, particularly in the presence of various salts, different pH values, temperatures, and agitation, and to perform their detailed structural and morphological characterization using biophysical methods (fluorescence spectroscopy, circular dichroism, ATR-FTIR, atomic force microscopy, and polyacrylamide gel electrophoresis). The stability of amyloid fibrils and hydrogels will be evaluated in the presence of proteolytic enzymes (pepsin, trypsin, and others), detergents such as SDS, and selected nanoparticles in order to assess their resistance and interactions in complex systems. The thesis also explores the potential applications of amyloid fibrils and hydrogels of both proteins in the food sector, either as nutritional supplements with added nutritional value or as carriers and stabilizers of hydrophobic bioactive compounds. The obtained results may contribute to a better understanding of the behavior of food-related amyloid structures under biologically relevant conditions and to elucidating their potential as next-generation nutritional preparations.