Cell interaction study of amyloid by using luminescent conjugated polythiophene: implication that amyloid
Tamotsu Zako1, Masafumi Sakono, Takahiro Kobayashi
1Bioengineering Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. zako@riken.jp
Chembiochem : a European Journal of Chemical Biology
|January 21, 2012
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.


