Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity.

@article{Ladiwala2012ConformationalDB,
  title={Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity.},
  author={Ali Reza A Ladiwala and Jeffrey Litt and Ravi S. Kane and Darryl S Aucoin and Steven Oliver Smith and Swarnim Ranjan and Judianne Davis and William E. Van Nostrand and Peter M Tessier},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 29},
  pages={24765-73}
}
Several protein conformational disorders (Parkinson and prion diseases) are linked to aberrant folding of proteins into prefibrillar oligomers and amyloid fibrils. Although prefibrillar oligomers are more toxic than their fibrillar counterparts, it is difficult to decouple the origin of their dissimilar toxicity because oligomers and fibrils differ both in terms of structure and size. Here we report the characterization of two oligomers of the 42-residue amyloid β (Aβ42) peptide associated with… CONTINUE READING
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