Nucleation-fibrillation dynamics of Aβ 1-40 peptides on liquid-solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor
作者： Hiroki Hamada , Hirotsugu Ogi , Kentaro Noi , Hisashi Yagi , Yuji Goto
关键词: Biophysics 、 Biosensor 、 Quartz crystal microbalance 、 Oligomer 、 Microscopy 、 Analytical chemistry 、 Total internal reflection fluorescence microscope 、 Nucleation 、 Adsorption 、 Quartz 、 Chemistry
摘要: We have successfully developed the total-internal-reflection-fluorescence microscopy combined with a quartz-crystal microbalance (TIRFM-QCM) biosensor, and monitored nucleation–fibrillation phenomenon of amyloid β1-40 peptide on naked quartz surface. The cross-β-sheet structures were visualized TIRFM using thioflavin-T (Th-T) label, other unlabeled aggregates detected through frequency change 58-MHz wireless-electrodeless QCM throughout aggregation reaction. response indicates significant adsorption peptides surface at early stage, which is followed by fibrillation. non-cross-β-sheet oligomers are first formed, nuclei appear in oligomer region, from fibrils originate elongate. two-color observation was performed after reaction Nile-red label as well ThT for identifying nucleation non-β-sheet regions. An model proposed.
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