MASAŘÍK, Michal, Agata STOBIECKA, René KIZEK, František JELEN, Zdeněk PECHAN, Wolfgang HOYER, Thomas JOVIN, Vinod SUBRAMANIAM and Emil PALEČEK. Sensitive electrochemical detection of native and aggregated alpha-synuclein protein involved in Parkinson's disease. Electroanalysis. Germany, Weinheim: Wiley-VCH Verlag GmbH & Co., 2004, vol. 16, 13-14, p. 1172-1181. ISSN 1040-0397. |
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@article{721759, author = {Masařík, Michal and Stobiecka, Agata and Kizek, René and Jelen, František and Pechan, Zdeněk and Hoyer, Wolfgang and Jovin, Thomas and Subramaniam, Vinod and Paleček, Emil}, article_location = {Germany, Weinheim}, article_number = {13-14}, keywords = {electrochemistry of proteins; alpha-synuclein aggregation; adsorptive transfer stripping; mercury and carbon electrodes; catalytic hydrogen evolution}, language = {eng}, issn = {1040-0397}, journal = {Electroanalysis}, title = {Sensitive electrochemical detection of native and aggregated alpha-synuclein protein involved in Parkinson's disease}, volume = {16}, year = {2004} }
TY - JOUR ID - 721759 AU - Masařík, Michal - Stobiecka, Agata - Kizek, René - Jelen, František - Pechan, Zdeněk - Hoyer, Wolfgang - Jovin, Thomas - Subramaniam, Vinod - Paleček, Emil PY - 2004 TI - Sensitive electrochemical detection of native and aggregated alpha-synuclein protein involved in Parkinson's disease JF - Electroanalysis VL - 16 IS - 13-14 SP - 1172-1181 EP - 1172-1181 PB - Wiley-VCH Verlag GmbH & Co. SN - 10400397 KW - electrochemistry of proteins KW - alpha-synuclein aggregation KW - adsorptive transfer stripping KW - mercury and carbon electrodes KW - catalytic hydrogen evolution N2 - The aggregation of alpha-synuclein, a 14 kDa protein, is involved in several human neurodegenerative disorders, including Parkinson's disease. We studied native and in vitro aggregated alpha-synuclein by circular dichroism (CD), atomic force microscopy (AFM) and electrochemical methods. We used constant current chronopotentiometric stripping analysis (CPSA) to measure hydrogen evolution catalyzed by alpha-synuclein (peak H) at hanging mercury drop electrodes (HMDE) and square-wave stripping voltammetry (SWSV) to monitor tyrosine oxidation at carbon paste electrodes (CPE). To decrease the volume of the analyte, most of the electrochemical measurements were performed by adsorptive transfer (medium exchange) from 3 - 6 muL drops of alpha-synuclein samples. With both CPE and HMDE we observed changes in electrochemical responses of alpha-synuclein corresponding to protein fibrillization detectable by CD, fluorescence and AFM. Aggregation-induced changes in peak H at HMDE were relatively large in strongly aggregated samples, suggesting that this electrochemical signal may find use in the analysis of early stages of alpha-synuclein aggregation. This assumption was documented by marked changes in the peak H potential and height in samples withdrawn at the end of the lag and the beginning of the elongation phase. Native alpha-synuclein can be detected down to subnanomolar concentrations by CPSA. ER -
MASAŘÍK, Michal, Agata STOBIECKA, René KIZEK, František JELEN, Zdeněk PECHAN, Wolfgang HOYER, Thomas JOVIN, Vinod SUBRAMANIAM and Emil PALEČEK. Sensitive electrochemical detection of native and aggregated alpha-synuclein protein involved in Parkinson's disease. \textit{Electroanalysis}. Germany, Weinheim: Wiley-VCH Verlag GmbH \&{} Co., 2004, vol.~16, 13-14, p.~1172-1181. ISSN~1040-0397.
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