Changes in interfacial properties of alpha-synuclein preceding
its aggregation

J 2008

Changes in interfacial properties of alpha-synuclein preceding its aggregation

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

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

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

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

Anotace

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.

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.

Citovat

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.

@article{807034,
   author = {Paleček, Emil and Ostatná, Veronika and Masařík, Michal and Bertoncini, Carlos and Jovin, Thomas},
   article_location = {Cambridge},
   article_number = {1},
   doi = {http://dx.doi.org/10.1039/b712812f},
   keywords = {ALPHA-SYNUCLEIN; DISEASE-ASSOCIATED MUTANTS; PARKINSONS-DISEASE; STRIPPING VOLTAMMETRY; NEURODEGENERATIVE DISORDERS; ELECTROCHEMICAL DETECTION; BIOACTIVE PEPTIDES; CARBON ELECTRODES; BETA-SYNUCLEIN; IN-VITRO; DYNAMICS},
   language = {eng},
   issn = {0003-2654},
   journal = {Analyst},
   title = {Changes in interfacial properties of alpha-synuclein preceding its aggregation},
   volume = {133},
   year = {2008}
}

TY  - JOUR
ID  - 807034
AU  - Paleček, Emil - Ostatná, Veronika - Masařík, Michal - Bertoncini, Carlos - Jovin, Thomas
PY  - 2008
TI  - Changes in interfacial properties of alpha-synuclein preceding its aggregation
JF  - Analyst
VL  - 133
IS  - 1
SP  - 76-84
EP  - 76-84
PB  - The Royal Society of Chemistry
SN  - 00032654
KW  - ALPHA-SYNUCLEIN
KW  - DISEASE-ASSOCIATED MUTANTS
KW  - PARKINSONS-DISEASE
KW  - STRIPPING VOLTAMMETRY
KW  - NEURODEGENERATIVE DISORDERS
KW  - ELECTROCHEMICAL DETECTION
KW  - BIOACTIVE PEPTIDES
KW  - CARBON ELECTRODES
KW  - BETA-SYNUCLEIN
KW  - IN-VITRO
KW  - DYNAMICS
N2  - 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.
ER  -

PALEČEK, Emil, Veronika OSTATNÁ, Michal MASAŘÍK, Carlos BERTONCINI a Thomas JOVIN. Changes in interfacial properties of alpha-synuclein preceding its aggregation. \textit{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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