Enhanced toxicity and cellular binding of a modified amyloid beta peptide with a methionine to valine substitution.

@article{Ciccotosto2004EnhancedTA,
  title={Enhanced toxicity and cellular binding of a modified amyloid beta peptide with a methionine to valine substitution.},
  author={Giuseppe Donato Ciccotosto and Deborah J Tew and Cyril C. Curtain and Danielle G Smith and Darryl P Carrington and Colin L. Masters and Ashley I. Bush and Robert Alan Cherny and Roberto Cappai and Kevin Jeffrey Barnham},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 41},
  pages={42528-34}
}
The amyloid beta peptide (Abeta) is toxic to neuronal cells, and it is probable that this toxicity is responsible for the progressive cognitive decline associated with Alzheimer's disease. However, the nature of the toxic Abeta species and its precise mechanism of action remain to be determined. It has been reported that the methionine residue at position 35 has a pivotal role to play in the toxicity of Abeta. We examined the effect of mutating the methionine to valine in Abeta42 (AbetaM35V… CONTINUE READING