Cell interaction study of amyloid by using luminescent conjugated polythiophene: implication that amyloid cytotoxicity is correlated with prolonged cellular binding

Chembiochem. 2012 Feb 13;13(3):358-63. doi: 10.1002/cbic.201100467. Epub 2012 Jan 19.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / chemistry*
  • Amyloid / pharmacology*
  • Animals
  • Binding Sites / drug effects
  • Cell Membrane / drug effects
  • Cell Survival / drug effects
  • HEK293 Cells
  • Humans
  • Luminescence*
  • PC12 Cells
  • Polymers / chemistry*
  • Rats
  • Spectrometry, Fluorescence
  • Structure-Activity Relationship
  • Thiophenes / chemistry*

Substances

  • Amyloid
  • Polymers
  • Thiophenes
  • polythiophene