SANS study of Amyloid β 1−40: Unfolded monomers in DMSO, multidimensional aggregates in water medium

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

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)385-391
Number of pages7
JournalPhysica A: Statistical Mechanics and its Applications
Volume517
DOIs
Publication statusPublished - Mar 1 2019

Keywords

  • Amyloid aggregation
  • Amyloid fibrils
  • SANS

ASJC Scopus subject areas

  • Statistics and Probability
  • Condensed Matter Physics

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