Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH.

@article{Klug2003BetaamyloidPO,
  title={Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH.},
  author={Genevieve M J A Klug and Dusan Losic and Supundi S Subasinghe and Marie-isabel Aguilar and Lisandra L Martin and David Henry Small},
  journal={European journal of biochemistry},
  year={2003},
  volume={270 21},
  pages={4282-93}
}
Amyloid protein (Abeta1-40) aggregation and conformation was examined using native and sodium dodecyl sulfate/polyacrylamide gel electrophoresis, and the results compared with those obtained by atomic force microscopy, and with Congo red binding, sedimentation and turbidity assays. The amount of Abeta aggregation measured was different, depending upon the method used. Incubation for 15 min at pH 5.0 or in the presence of Fe2+, Cu2+ or Zn2+ did not alter the level of Abeta oligomers observed on… CONTINUE READING