Structural Properties of Pore-Forming Oligomers of α-Synuclein

被引：158

作者：

Kim, Hai-Young ^{[1
]}

Cho, Min-Kyu ^{[1
]}

Kumar, Ashutosh ^{[1
]}

Maier, Elke ^{[5
]}

Siebenhaar, Carsten ^{[1
]}

Becker, Stefan ^{[1
]}

Fernandez, Claudio O. ^{[3
]}

Lashuel, Hilal A. ^{[4
]}

Benz, Roland ^{[5
]}

Lange, Adam ^{[1
]}

Zweckstetter, Markus ^{[1
,2
]}

机构：

[1] Max Planck Inst Biophys Chem, Dept NMR Based Struct Biol, D-37077 Gottingen, Germany

[2] DFG Res Ctr Mol Physiol Brain, D-37073 Gottingen, Germany

[3] Univ Nacl Rosario, Inst Biol Mol & Cellular Rosario, RA-2000 Rosario, Santa Fe, Argentina

[4] Ecole Polytech Fed Lausanne, Brain Mind Inst, CH-1015 Lausanne, Switzerland

[5] Jacobs Univ Bremen, Sch Sci & Engn, D-28759 Bremen, Germany

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 47期

关键词：

AMYLOID BETA-PEPTIDE; SOLID-STATE NMR; ALZHEIMERS-DISEASE; NEURODEGENERATIVE DISEASE; FLAVONOID BAICALEIN; SECONDARY STRUCTURE; PROTEIN; FIBRILS; CHANNELS; DYNAMICS;

D O I：

10.1021/ja9077599

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Soluble oligomers are potent toxins in many neurodegenerative diseases, but little is known about the structure of soluble oligomers and their structure-toxicity relationship. Here we prepared on-pathway oligomers of the 140-residue protein alpha-synuclein, a key player in Parkinson's disease, at concentrations an order of magnitude higher than previously possible. The oligomers form ion channels with well-defined conductance states in a variety of membranes, and their beta-structure differs from that of amyloid fibrils of alpha-synuclein.

引用

页码：17482 / 17489

页数：8

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