RNDr. Miroslav Gančár, PhD.
researcher
Amyloid aggregation of proteins
Watsonova 47
040 01 Košice
Slovak Republic
@:
EDUCATION & TRAINING
Ph.D. STUDY IN BIOPHYSICS (EQF level 8) – Pavol Jozef Šafárik University in Košice, Faculty of Science, Department of Biophysics and Institute of Experimental Physics, Department of Biophysics, Slovak Academy of Sciences in Košice, Slovakia
DISSERTATION THESIS – Amyloid self-assembly of proteins
◦ in vitro study of protein amyloid self-assembly (conformational changes, kinetics, mechanism)
◦ design and evaluation of potential amyloid inhibitors (small organic molecules, multi-target directed ligands, surface modified nanoparticles)
MASTER'S STUDY IN BIOCHEMISTRY (EQF level 7) – Pavol Jozef Šafárik University in Košice, Faculty of Science, Department of Biochemistry
MASTER THESIS – Catalytic properties of glucose oxidase
◦ research of the catalytic properties of glucose oxidase for biosensor production
◦ detailed examination of glucose oxidation mechanism - implementation of potentiometry and fluorimetry for the determination of glucose content in sweetened solutions and soda
CURRENT RESEARCH INTEREST
◦ My research focuses on several different aspects of protein amyloid aggregation – specific poly/peptide self-assembly process associated with the pathogenesis of many diseases such as Alzheimer's and Parkinson's diseases and type II diabetes
◦ The understanding of the amyloid aggregation of poly/peptides: (a) the specific mechanisms of poly/peptide aggregation, (b) the hierarchical structure of the poly/peptide amyloids from the atomistic to mesoscopic scale and (c) the physical properties of the amyloids in the context of their surrounding environment (biological or artificial)
◦ Self-assembled poly/peptide amyloid nanostructures.
◦ Study of low-molecular substances counteracting amyloid aggregation for their ability (a) to stabilize toxic amyloid precursors; (b) to prevent the growth of toxic oligomers; (c) to inhibit fibril growth and deposition; (d) to disassemble preformed fibrils; and (e) to favour amyloid clearance
◦ Of particular interest is the surface-modified nanoparticles' role in the depolymerization of amyloid aggregates or amyloid aggregation inhibition
Ph.D. STUDY IN BIOPHYSICS (EQF level 8) – Pavol Jozef Šafárik University in Košice, Faculty of Science, Department of Biophysics and Institute of Experimental Physics, Department of Biophysics, Slovak Academy of Sciences in Košice, Slovakia
DISSERTATION THESIS – Amyloid self-assembly of proteins
◦ in vitro study of protein amyloid self-assembly (conformational changes, kinetics, mechanism)
◦ design and evaluation of potential amyloid inhibitors (small organic molecules, multi-target directed ligands, surface modified nanoparticles)
MASTER'S STUDY IN BIOCHEMISTRY (EQF level 7) – Pavol Jozef Šafárik University in Košice, Faculty of Science, Department of Biochemistry
MASTER THESIS – Catalytic properties of glucose oxidase
◦ research of the catalytic properties of glucose oxidase for biosensor production
◦ detailed examination of glucose oxidation mechanism - implementation of potentiometry and fluorimetry for the determination of glucose content in sweetened solutions and soda
CURRENT RESEARCH INTEREST
◦ My research focuses on several different aspects of protein amyloid aggregation – specific poly/peptide self-assembly process associated with the pathogenesis of many diseases such as Alzheimer's and Parkinson's diseases and type II diabetes
◦ The understanding of the amyloid aggregation of poly/peptides: (a) the specific mechanisms of poly/peptide aggregation, (b) the hierarchical structure of the poly/peptide amyloids from the atomistic to mesoscopic scale and (c) the physical properties of the amyloids in the context of their surrounding environment (biological or artificial)
◦ Self-assembled poly/peptide amyloid nanostructures.
◦ Study of low-molecular substances counteracting amyloid aggregation for their ability (a) to stabilize toxic amyloid precursors; (b) to prevent the growth of toxic oligomers; (c) to inhibit fibril growth and deposition; (d) to disassemble preformed fibrils; and (e) to favour amyloid clearance
◦ Of particular interest is the surface-modified nanoparticles' role in the depolymerization of amyloid aggregates or amyloid aggregation inhibition