Dissociation of amyloid fibrils of α-synuclein in supercooled water

被引：33

作者：

Kim, Hai-Young ^{[1
]}

Cho, Min-Kyu ^{[1
]}

Riedel, Dietmar ^{[1
]}

Fernandez, Claudio O. ^{[3
]}

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-37077 Gottingen, Germany

[3] Univ Nacl Rosario, Inst Biol Mol & Celular Rosario, RA-2000 Rosario, Argentina

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 27期

关键词：

alpha-synuclein; amyloid fibrils; electron microscopy; NMR spectroscopy; proteins;

D O I：

10.1002/anie.200800342

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) Out in the cold: Amyloid fibrils formed by the protein α-synuclein, one of the key players in Parkinson's disease, are rapidly dissociated in supercooled water at -15°C (see TEM images), conditions in which many globular proteins remain folded. NMR studies indicate that the weakening of hydrophobic and electrostatic interactions contribute to the cold-induced destabilization of the amyloid fibrils. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：5046 / 5048

页数：3

共 23 条

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