کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10537544 962777 2014 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation
چکیده انگلیسی
The accumulation of protein aggregates containing amyloid fibrils, with α-synuclein being the main component, is a pathological hallmark of Parkinson's disease (PD). Molecules which prevent the formation of amyloid fibrils or disassociate the toxic aggregates are touted as promising strategies to prevent or treat PD. In the present study, in vitro Thioflavin T fluorescence assays and transmission electron microscopy imaging results showed that gallic acid (GA) potently inhibits the formation of amyloid fibrils by α-synuclein. Ion mobility-mass spectrometry demonstrated that GA stabilises the extended, native structure of α-synuclein, whilst NMR spectroscopy revealed that GA interacts with α-synuclein transiently.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1844, Issue 9, September 2014, Pages 1481-1485
نویسندگان
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