| Abstract |
The thesis will be oriented to development of new high-performance electromigration methods, affinity capillary electrophoresis and affinity open-tubular capillary electrochromatography, and on their application to investigation of non-covalent interactions of biologically active peptides, proteins, nucleosides, nucleotides and other biomolecules with low- or high-molecular-mass ligands or receptors. New procedures will be developed for quantitative characterization of both weak and strong interactions of biomolecules in a free solution or on a solid-liquid interface. Interactions of biomolecules, e.g. hormones or drugs with receptors, enzymes with substrates or inhibitors, and ionophores with ions in the free solution will be investigated by different modes of affinity capillary electrophoresis. Interactions of biomolecules on the solid-liquid interface will be studied by affinity open tubular capillary electrochromatography with ligands or receptors immobilized on the inner wall of the fused silica capillary. Strength of the interactions of biomolecules will be quantified by the stability constants of their complexes. |
