Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für biophysikalische Chemie     Collection: Molekulare Biologie (Dr. Thomas M. Jovin)     Display Documents



  history
ID: 174633.0, MPI für biophysikalische Chemie / Molekulare Biologie (Dr. Thomas M. Jovin)
Sensitive electrochemical detection of native and aggregated α-synuclein protein involved in Parkinson's Disease
Authors:Masarik, M.; Stobiecka, A.; Kizek, R.; Jelen, F.; Pechan, Z.; Hoyer, W.; Jovin, T. M.; Subramaniam, V.; Palecek, E.
Language:English
Date of Publication (YYYY-MM-DD):2004-06-30
Title of Journal:Electroanalysis
Volume:16
Issue / Number:13-14
Start Page:1172
End Page:1181
Sequence Number of Article:doi:10.1002/elan.200403009
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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 This assumption was documented by marked changes in the peak H potential and height in samples withdrawn at the end of the lag and the beginning of the elongation phase.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.
Free Keywords:Electrochemistry of proteins, α-synuclein aggregation, Adsorptive transfer stripping, Mercury and carbon electrodes, Catalytic hydrogen evolution
Last Change of the Resource (YYYY-MM-DD):2004-08-16
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Thomas Jovin / 060
External Affiliations:Institute of Biophysics of the Academy of Sciences of the Czech Republic, Kralovopolska 135, 612 65 Brno, Czech Pepublic; Department of Chemistry and Biochemistry, Faculty of Agronomy, Mendel University of Agriculture and Forestry, Zemedelska 1, 613 00 Brno, Czech Republic; Biophysical Engineering Group, Faculty of Science and Technology, University of Twente, PO Box 217, 7500 AE Enschede, The Netherlands
Identifiers:URL:http://www3.interscience.wiley.com/cgi-bin/fulltex...
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.