Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions.

  title={Perturbation of the stability of amyloid fibrils through alteration of electrostatic interactions.},
  author={Sarah L. Shammas and Tuomas P. J. Knowles and Andrew J Baldwin and Cait E. MacPhee and Mark Edward Welland and Christopher M. Dobson and Glyn L. Devlin},
  journal={Biophysical journal},
  volume={100 11},
The self-assembly of proteins and peptides into polymeric amyloid fibrils is a process that has important implications ranging from the understanding of protein misfolding disorders to the discovery of novel nanobiomaterials. In this study, we probe the stability of fibrils prepared at pH 2.0 and composed of the protein insulin by manipulating electrostatic interactions within the fibril architecture. We demonstrate that strong electrostatic repulsion is sufficient to disrupt the hydrogen… CONTINUE READING

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