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Cell interaction study of amyloid by using luminescent conjugated polythiophene: implication that amyloid cytotoxicity is correlated with prolonged cellular binding |
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| Authors: | Zako Tamotsu Sakono Masafumi Kobayashi Takahiro Sörgjerd Karin Nilsson K Peter R Hammarström Per Lindgren Mikael Maeda Mizuo |
| Affiliation: | Bioengineering Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. zako@riken.jp |
| Abstract: | Needles and noodles: Studying amyloid toxicity is important for understanding protein misfolding diseases. Using a luminescent conjugated polythiophene, we found that cell binding of nontoxic filamentous amyloids of insulin and β2-microglobulin was less efficient than that of toxic fibrillar amyloids; this suggests a correlation between amyloid toxicity and cell binding. |
| Keywords: | amyloid beta‐peptides cell binding cytotoxicity luminescent conjugated polythiophene (LCP) protein folding |
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