| MASAŘÍK, Michal, Agata STOBIECKA, René KIZEK, František JELEN, Zdeněk PECHAN, Wolfgang HOYER, Thomas JOVIN, Vinod SUBRAMANIAM a 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, roč. 16, 13-14, s. 1172-1181. ISSN 1040-0397. |
Další formáty:
BibTeX
LaTeX
RIS
@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 a 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, roč.~16, 13-14, s.~1172-1181. ISSN~1040-0397.
|
