English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Sensitive electrochemical detection of native and aggregated α-synuclein protein involved in Parkinson's Disease

MPS-Authors
/persons/resource/persons15252

Hoyer,  W.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15286

Jovin,  T. M.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15895

Subramaniam,  V.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Masarik, M., Stobiecka, A., Kizek, R., Jelen, F., Pechan, Z., Hoyer, W., et al. (2004). Sensitive electrochemical detection of native and aggregated α-synuclein protein involved in Parkinson's Disease. Electroanalysis, 16(13-14): doi:10.1002/elan.200403009, pp. 1172-1181. Retrieved from http://www3.interscience.wiley.com/cgi-bin/fulltext/109086191/PDFSTART.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-ED00-C
Abstract
The aggregation of α-synuclein, a 14 kDa protein, is involved in several human neurodegenerative disorders, including Parkinson´s disease. We studied native and in vitro aggregated α-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 α-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 μL drops of α-synuclein samples. With both CPE and HMDE we observed changes in electrochemical responses of a-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 α-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 α-synuclein can be detected down to subnanomolar concentrations by CPSA.