Compressibility of insulin amyloid fibrils determined by X-ray diffraction in a diamond anvil cell

Meersman, Filip;Cabrera, Raul Quesada;McMillan, Paul F.;Dmitriev, Vladimir
(2009) 47th Meeting of the European-High-Pressure-Research-Group (EHPRG 47) — Location: Univ Pierre & Marie Curie, Cordeliers Campus, Paris(France) (6.September.2009)

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  • Meersman, FilipUCLouvain
    Author
  • Cabrera, Raul QuesadaUCLouvain
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  • McMillan, Paul F.UCLouvain
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  • Dmitriev, Vladimir
    Author
Abstract
Amyloid fibrils are fibrous structures that originate from the self-assembly of polypeptides. Their formation is linked to debilitating diseases associated with protein misfolding, including Alzheimer's disease and type-II diabetes. In recent years, it has been suggested that such protein and polypeptide fibrils might provide useful novel nanomaterials. Here, we present the results of a study on the high pressure stability and compressibility of mature amyloid fibrils of insulin by synchrotron X-ray diffraction in a diamond anvil cell. The diffraction results allow a direct estimation of the elastic modulus and the corresponding compression of the cross- structure along the fiber axis. The average hydrogen bond compressibility is comparable to that in native proteins, suggesting that the fibrils are well-packed.
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Meersman, F., Cabrera, R. Q., McMillan, P. F., & Dmitriev, V. (2009). Compressibility of insulin amyloid fibrils determined by X-ray diffraction in a diamond anvil cell. High Pressure Research : an international journal, 29(4), 665-670. https://doi.org/10.1080/08957950903350975 (Original work published 2009)