J 2008

Changes in interfacial properties of alpha-synuclein preceding its aggregation

PALEČEK, Emil, Veronika OSTATNÁ, Michal MASAŘÍK, Carlos BERTONCINI, Thomas JOVIN et. al.

Basic information

Original name

Changes in interfacial properties of alpha-synuclein preceding its aggregation

Name in Czech

Změny v povrchových vlastnostech předcházejících agregaci alfa-synukleinu

Authors

PALEČEK, Emil (203 Czech Republic, belonging to the institution), Veronika OSTATNÁ (703 Slovakia), Michal MASAŘÍK (203 Czech Republic, guarantor, belonging to the institution), Carlos BERTONCINI (276 Germany) and Thomas JOVIN (276 Germany)

Edition

Analyst, Cambridge, The Royal Society of Chemistry, 2008, 0003-2654

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10405 Electrochemistry

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 3.761

RIV identification code

RIV/00216224:14110/08:00051089

Organization unit

Faculty of Medicine

DOI

UT WoS

000251684300019

Keywords in English

ALPHA-SYNUCLEIN; DISEASE-ASSOCIATED MUTANTS; PARKINSONS-DISEASE; STRIPPING VOLTAMMETRY; NEURODEGENERATIVE DISORDERS; ELECTROCHEMICAL DETECTION; BIOACTIVE PEPTIDES; CARBON ELECTRODES; BETA-SYNUCLEIN; IN-VITRO; DYNAMICS

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Tags

International impact
Změněno: 10/4/2012 14:44, Mgr. Michal Petr

Abstract

ORIG CZ

V originále

Parkinson's disease (PD) is associated with the formation and deposition of amyloid fibrils of the protein alpha-synuclein (AS). It has been proposed that oligomeric intermediates on the pathway to fibrilization rather than the fibrils themselves are the pathogenic agents of PD, but efficient methods for their detection are lacking. We have studied the interfacial properties of wild-type AS and the course of its aggregation in vitro using electrochemical analysis and dynamic light scattering. The oxidation signals of tyrosine residues of AS at carbon electrodes and the ability of fibrils to adsorb and catalyze hydrogen evolution at hanging mercury drop electrodes (HMDEs) decreased during incubation. HMDEs were particularly sensitive to pre-aggregation changes in AS. Already after 1 h of a standard aggregation assay in vitro (stirring at 37 degrees C), the electrocatalytic peak H increased greatly and shifted to less negative potentials. Between 3 and 9 h of incubation, an interval during which dynamic light scattering indicated AS oligomerization, peak H diminished and shifted to more negative potentials, and AS adsorbability decreased. We tentatively attribute the very early changes in the interfacial behavior of the protein after the first few hours of incubation to protein destabilization with disruption of long-range interactions. The subsequent changes can be related to the onset of oligomerization. Our results demonstrate the utility of electrochemical methods as new and simple tools for the investigation of amyloid formation.

In Czech

Parkinsonova choroba je spojena s ukládáním amyloidních fibril proteinu zvaného alfa-synuklein. Bylo prokázáno že oligomerní struktury tohoto proteinu jsou mnohem více patogenní než samotné zralé fibrily. Stále však chybí metody pro jejich včasnou detekci. My jsme studovali povrchové vlastnosti alfa-synukleinu pomocí elektrochemické analýzy. Prokázali jsme, že tyto metody jsou schopny agregaci tohoto proteinu odhalit mnohem časněji než standardně užívané metody jako je CD nebo AFM.