Unfolding/denaturation and aggregation of proteins viewed by electrochemical methods
Pioneering work of the group headed by prof. E. Paleček in the field of electrochemical analysis of proteins based on their electrocatalytic activity giving rise to “peak H” at mercury-based electrodes. The peak H responds sensitively to changes in the protein structure. In contrast to traditional view considering proteins adsorbed at mercury electrode surface inherently denatured, it has been shown that adsorbed proteins retain (at least partly) their folded structure. Sensitivity of the peak H to protein unfolding (denaturation) can be utilized to monitor unfolding transitions in solution and at the electrode surface. Moreover, the peak H has been used to monitor pre-aggregation and aggregation processes of a-synuclein, a protein the aggregation of which is connected with Parkinson’s disease. Electrochemistry has proved sensitive particularly to changes taking place in early stages of the aggregation process, thus representing a useful tool for e.g., seeking substances (potential drugs) affecting the aggregation trigger.
V. Ostatna, F. Kuralay, L. Trnkova, and E. Palecek, Constant current chronopotentiometry and voltammetry of native and denatured serum albumin at mercury and carbon electrodes. Electroanalysis 20, 1406-1413, 2008.
V. Ostatna, and E. Palecek, Native, denatured and reduced BSA - Enhancement of chronopotentiometric peak H by guanidinium chloride. Electrochimica Acta 53, 4014-4021, 2008.
E. Palecek, and V. Ostatna, Potential-dependent surface denaturation of BSA in acid media. Analyst 134, 2076-2080, 2009.
E. Palecek, and V. Ostatna, Ionic strength-dependent structural transition of proteins at electrode surfaces. Chemical Communications 13, 1685-1687, 2009.
E. Palecek, V. Ostatna, M. Masarik, K. Bertoncini, and T.M. Jovin, Changes in interfacial properties of a-synuclein preceding its aggregation. Analyst 133, 76-84, 2008.