PALEČEK, Emil, Veronika OSTATNÁ, Michal MASAŘÍK, Carlos BERTONCINI and Thomas JOVIN. Changes in interfacial properties of alpha-synuclein preceding its aggregation. Analyst. Cambridge: The Royal Society of Chemistry, 2008, vol. 133, No 1, p. 76-84. ISSN 0003-2654. Available from: https://dx.doi.org/10.1039/b712812f.
Other formats:   BibTeX LaTeX RIS
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
Original language English
Type of outcome Article in a journal
Field of Study 10405 Electrochemistry
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 3.761
RIV identification code RIV/00216224:14110/08:00051089
Organization unit Faculty of Medicine
Doi http://dx.doi.org/10.1039/b712812f
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
Tags ALPHA-SYNUCLEIN, BETA-SYNUCLEIN, BIOACTIVE PEPTIDES, carbon electrodes, DISEASE-ASSOCIATED MUTANTS, dynamics, electrochemical detection, in-vitro, NEURODEGENERATIVE DISORDERS, PARKINSONS-DISEASE, stripping voltammetry
Tags International impact
Changed by Changed by: Mgr. Michal Petr, učo 65024. Changed: 10/4/2012 14:44.
Abstract
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.
Abstract (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.
PrintDisplayed: 25/4/2024 16:01