English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

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

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.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-ED00-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-DAAA-C
Genre: Journal Article

Files

show Files
hide Files
:
174633.pdf (Publisher version), 0B
 
File Permalink:
-
Name:
174633.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), Göttingen; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Masarik, M., Author
Stobiecka, A., Author
Kizek, R., Author
Jelen, F., Author
Pechan, Z., Author
Hoyer, W.1, Author              
Jovin, T. M.1, Author              
Subramaniam, V.1, Author              
Palecek, E., Author
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

Content

show
hide
Free keywords: Electrochemistry of proteins, α-synuclein aggregation, Adsorptive transfer stripping, Mercury and carbon electrodes, Catalytic hydrogen evolution
 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.

Details

show
hide
Language(s): eng - English
 Dates: 2004-08-162004-06-30
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Electroanalysis
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 16 (13-14) Sequence Number: doi:10.1002/elan.200403009 Start / End Page: 1172 - 1181 Identifier: -