• Medicine
  • Published in
    Proceedings of the National…
    1999

In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation.

@article{Kowalewski1999InSA,
  title={In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation.},
  author={Tomasz Kowalewski and David M Holtzman},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1999},
  volume={96 7},
  pages={
          3688-93
        }
}
We have applied in situ atomic force microscopy to directly observe the aggregation of Alzheimer's beta-amyloid peptide (Abeta) in contact with two model solid surfaces: hydrophilic mica and hydrophobic graphite. The time course of aggregation was followed by continuous imaging of surfaces remaining in contact with 10-500 microM solutions of Abeta in PBS (pH 7.4). Visualization of fragile nanoscale aggregates of Abeta was made possible by the application of a tapping mode of imaging, which… CONTINUE READING

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