Podrobný výpis o publikaci

PALEČEK, Emil, Veronika OSTATNÁ, Michal MASAŘÍK, Carlos BERTONCINI a Thomas JOVIN. Changes in interfacial properties of alpha-synuclein preceding its aggregation. Analyst. Cambridge: The Royal Society of Chemistry, 2008, roč. 133, č. 1, s. 76-84. ISSN 0003-2654. Dostupné z: https://dx.doi.org/10.1039/b712812f.

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Základní údaje
Originální název	Changes in interfacial properties of alpha-synuclein preceding its aggregation
Název česky	Změny v povrchových vlastnostech předcházejících agregaci alfa-synukleinu
Autoři	PALEČEK, Emil (203 Česká republika, domácí), Veronika OSTATNÁ (703 Slovensko), Michal MASAŘÍK (203 Česká republika, garant, domácí), Carlos BERTONCINI (276 Německo) a Thomas JOVIN (276 Německo).
Vydání	Analyst, Cambridge, The Royal Society of Chemistry, 2008, 0003-2654.

Další údaje
Originální jazyk	angličtina
Typ výsledku	Článek v odborném periodiku
Obor	10405 Electrochemistry
Stát vydavatele	Velká Británie a Severní Irsko
Utajení	není předmětem státního či obchodního tajemství
Impakt faktor	Impact factor: 3.761
Kód RIV	RIV/00216224:14110/08:00051089
Organizační jednotka	Lékařská fakulta
Doi	http://dx.doi.org/10.1039/b712812f
UT WoS	000251684300019
Klíčová slova anglicky	ALPHA-SYNUCLEIN; DISEASE-ASSOCIATED MUTANTS; PARKINSONS-DISEASE; STRIPPING VOLTAMMETRY; NEURODEGENERATIVE DISORDERS; ELECTROCHEMICAL DETECTION; BIOACTIVE PEPTIDES; CARBON ELECTRODES; BETA-SYNUCLEIN; IN-VITRO; DYNAMICS
Štítky	ALPHA-SYNUCLEIN, BETA-SYNUCLEIN, BIOACTIVE PEPTIDES, carbon electrodes, DISEASE-ASSOCIATED MUTANTS, dynamics, electrochemical detection, in-vitro, NEURODEGENERATIVE DISORDERS, PARKINSONS-DISEASE, stripping voltammetry
Příznaky	Mezinárodní význam
Změnil	Změnil: Mgr. Michal Petr, učo 65024. Změněno: 10. 4. 2012 14:44.

Anotace
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.

Anotace

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.

Anotace česky
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.

Anotace česky

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.