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

Title
Observation of multi-step conformation switching in β-amyloid peptide aggregation by fluorescence resonance energy transfer
Authors
Kim J.Lee M.
Ewha Authors
이민영
SCOPUS Author ID
이민영scopus
Issue Date
2004
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
vol. 316, no. 2, pp. 393 - 397
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
We have observed the conformation switching of Aβ11-25 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 β-sheet in fibrils. We first identified the critical micelle concentration of Aβ 11-25 that occurs at ca. 3μM for pH 5.0 and ca. 70μM for pH 7.4. Our experimental results show clearly that the end-to-end distance of micellar Aβ11-25 becomes much shorter than that of the collapsed coil or fibril structure. © 2004 Elsevier Inc. All rights reserved.
DOI
10.1016/j.bbrc.2004.02.059
Appears in Collections:
자연과학대학 > 화학·나노과학전공 > Journal papers
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