Characterization and real-time imaging of the FTLD-related protein aggregation induced by amyloidogenic peptides
Ruei-Yu He1, Yi-Chen Huang, Chao-Wei Chiang
1Institute of Chemistry, Academia Sinica, No. 128, Sec. 2, Academia Road, Nankang, Taipei 115, Taiwan. jthuang@gate.sinica.edu.tw leehm@chem.sinica.edu.tw.
Chemical Communications (Cambridge, England)
|April 24, 2015
Abstract:
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.
Related Concept Videos
03:03Amyloid Fibrils
13.1K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
13.1K
03:03Amyloid Fibrils
7.0K
7.0K