Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide.

@article{Green2004AtomicFM,
  title={Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide.},
  author={Janelle D Green and Laurent Kreplak and Claire S Goldsbury and X Li Blatter and Martin Stolz and Garth J S Cooper and Anna Seelig and Joerg Kistler and Ueli Aebi},
  journal={Journal of molecular biology},
  year={2004},
  volume={342 3},
  pages={877-87}
}
To date, over 20 peptides or proteins have been identified that can form amyloid fibrils in the body and are thought to cause disease. The mechanism by which amyloid peptides cause the cytotoxicity observed and disease is not understood. However, one of the major hypotheses is that amyloid peptides cause membrane perturbation. Hence, we have studied the interaction between lipid bilayers and the 37 amino acid residue polypeptide amylin, which is the primary constituent of the pancreatic amyloid… CONTINUE READING

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