Characterization and real-time imaging of the FTLD-related protein aggregation induced by amyloidogenic peptidesElectronic supplementary information (ESI) available: Experimental details, the mass spectrum, cell-free experiments and real-time fluorescence images. See DOI: 10.1039/c5cc00513b

We identify a new amyloidogenic peptide from the glutamine/asparagine-rich region of the FTLD-related protein (TDP-43), which can seed both the full-length and N-terminus-truncated TDP-43. Through the microinjection and real-time fluorescence imaging, we also found that this novel peptide could trig...

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Main Authors He, Ruei-Yu, Huang, Yi-Chen, Chiang, Chao-Wei, Tsai, Yu-Ju, Ye, Ting-Juan, Gao, Hua-De, Wu, Chu-Ya, Lee, Hsien-Ming, Huang, Joseph Jen-Tse
Format Journal Article
LanguageEnglish
Published 07.05.2015
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Summary:We identify a new amyloidogenic peptide from the glutamine/asparagine-rich region of the FTLD-related protein (TDP-43), which can seed both the full-length and N-terminus-truncated TDP-43. Through the microinjection and real-time fluorescence imaging, we also found that this novel peptide could trigger cell apoptosis and initiate TDP-43 aggregation in the cytosol. Q/N- and G-rich polypeptides from the TDP-43 C-terminus formed amyloid fibers in vitro and induced the aggregation of the transfected TDP-43-EGFP in live cells.
Bibliography:10.1039/c5cc00513b
Electronic supplementary information (ESI) available: Experimental details, the mass spectrum, cell-free experiments and real-time fluorescence images. See DOI
ISSN:1359-7345
1364-548X
DOI:10.1039/c5cc00513b