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  • Title: Observation of multi-step conformation switching in beta-amyloid peptide aggregation by fluorescence resonance energy transfer.
    Author: Kim J, Lee M.
    Journal: Biochem Biophys Res Commun; 2004 Apr 02; 316(2):393-7. PubMed ID: 15020230.
    Abstract:
    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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