Nucleation–fibrillation dynamics of Aβ1-40 peptides on liquid–solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor

@inproceedings{Hamada2015NucleationfibrillationDO,
  title={Nucleation–fibrillation dynamics of Aβ1-40 peptides on liquid–solid surface studied by total-internal-reflection fluorescence microscopy coupled with quartz-crystal microbalance biosensor},
  author={Hiroki Hamada and Hirotsugu Ogi and Kentaro Noi and Hisashi Yagi and Yuji Goto and Masahiko Hirao},
  year={2015}
}
We have successfully developed the total-internal-reflection-fluorescence microscopy combined with a quartz-crystal microbalance (TIRFM-QCM) biosensor, and monitored the nucleation–fibrillation phenomenon of amyloid β1-40 peptide on the naked quartz surface. The cross-β-sheet structures were visualized with the TIRFM using the thioflavin-T (Th-T) label, and other unlabeled aggregates were detected through the frequency change of the 58-MHz wireless-electrodeless QCM throughout the aggregation… CONTINUE READING

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