Trehalose inhibits fibrillation of A53T mutant alpha-synuclein and disaggregates existing fibrils.
Arch Biochem Biophys
; 523(2): 144-50, 2012 Jul 15.
Article
em En
| MEDLINE
| ID: mdl-22575388
ABSTRACT
The aggregation of alpha-synuclein (AS) is pivotally implicated in the development of Parkinson's disease (PD), inhibiting this process might be effective in treating PD. Here, by using circular dichroism spectroscopy, thioflavin T fluorescence, and atomic force microscopy, we found that trehalose at low concentration disaggregates preformed A53T AS protofibrils and fibrils into small aggregates or even random coil structure, while trehalose at high concentration slows down the structural transition into ß-sheet structure and completely prevents the formation of mature A53T AS fibrils. Further work in vivo will be needed to evaluate its potential as a novel strategy for treating PD.
Texto completo:
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Trealose
/
Proteínas Mutantes
/
Alfa-Sinucleína
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Multimerização Proteica
/
Mutação
Limite:
Humans
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article