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Biochem Biophys Res Commun. 2004 Apr 2;316(2):393-7.

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

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  • 1Laboratory of Fluorescence Nanoscopy, Department of Chemistry, and Division of Molecular Life Sciences, Ewha Womans University, Seoul 120-750, Republic of Korea.


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 beta-sheet in fibrils. We first identified the critical micelle concentration of Abeta(11-25) that occurs at ca. 3 microM for pH 5.0 and ca. 70 microM 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.

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