Observation of multi-step conformation switching in β-amyloid peptide aggregation by fluorescence resonance energy transfer

被引：22

作者：

Kim, J

Lee, M ^{[1
]}

机构：

[1] Ewha Womans Univ, Dept Chem, Lab Fluorescence Nanoscopy, Seoul 120750, South Korea

[2] Ewha Womans Univ, Div Mol Life Sci, Seoul 120750, South Korea

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 316卷 / 02期

关键词：

D O I：

10.1016/j.bbrc.2004.02.059

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have observed the conformation switching of Abeta(11-25) in the course of amyloid aggregation by employing time-resolved fluorescence resonance energy transfer (FRET). The amyloid peptides undergo multi-step conformational changes during self-assembling such as random coil (monomers), collapsed coil (multimers), micellar structure, and extended P-sheet in fibrils. We first identified the critical micelle concentration of Abeta(11-25) that occurs at ca. 3 muM for pH 5.0 and ca. 70 muM for pH 7.4. Our experimental results show clearly that the end-to-end distance of micellar Abeta(11-25) becomes much shorter than that of the collapsed coil or fibril structure. (C) 2004 Elsevier Inc. All rights reserved.

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页码：393 / 397

页数：5

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