کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10870848 1074023 2014 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes
چکیده انگلیسی
The intrinsically disordered protein α-synuclein (αSN) is linked to Parkinson's Disease and forms both oligomeric species and amyloid fibrils. The N-terminal part of monomeric αSN interacts strongly with membranes and αSN cytotoxicity has been attributed to oligomers' ability to interact with and perturb membranes. We show that membrane folding of monomeric wt αSN and N-terminally truncated variants correlates with membrane permeabilization. Further, the first 11 N-terminal residues are crucial for monomers' and oligomers' interactions with and permeabilization of membranes. We attribute oligomer permeabilization both to cooperative electrostatic interactions through the N-terminus and interactions mediated by hydrophobic regions in the oligomer.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 588, Issue 3, 31 January 2014, Pages 497-502
نویسندگان
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