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SANS study of Amyloid β1−40: Unfolded monomers in DMSO, multidimensional aggregates in water medium

Author

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  • Festa, Giulia
  • Sancesario, Giulia
  • Corsaro, Carmelo
  • Longo, Sveva
  • Mallamace, Domenico
  • Fazio, Enza
  • Arcidiacono, Laura
  • Sakai, Victoria Garcia
  • Senesi, Roberto
  • Sancesario, Giuseppe
  • Mallamace, Francesco
  • Andreani, Carla

Abstract

Neurodegenerative diseases such as Alzheimer’s are characterized by neuritic plaques throughout the brain gray matter, associated with neurofibrillary tangles and neuron loss. These plaques are formed by abnormal aggregation of amyloid beta (Aβ) peptide into insoluble fibrils. In the present work we study the Aβ1−40 peptide in the three aggregations states – monomers, oligomers and fibrils – via small angle neutron scattering (SANS) technique. The size of the three forms as well as their fractal nature are investigated at physiologic conditions. Our results evidence that the Aβ1−40 peptide has a good aggregation capability but can also adopt an unfolded conformation in particular conditions, as for example, when incubated in DMSO.

Suggested Citation

  • Festa, Giulia & Sancesario, Giulia & Corsaro, Carmelo & Longo, Sveva & Mallamace, Domenico & Fazio, Enza & Arcidiacono, Laura & Sakai, Victoria Garcia & Senesi, Roberto & Sancesario, Giuseppe & Mallam, 2019. "SANS study of Amyloid β1−40: Unfolded monomers in DMSO, multidimensional aggregates in water medium," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 517(C), pages 385-391.
    • Handle: RePEc:eee:phsmap:v:517:y:2019:i:c:p:385-391
    DOI: 10.1016/j.physa.2018.11.027
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    Cited by:

    1. Corsaro, Carmelo & Mallamace, Domenico & Neri, Giulia & Fazio, Enza, 2021. "Hydrophilicity and hydrophobicity: Key aspects for biomedical and technological purposes," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 580(C).

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