Aggregation States of Aβ1-40, Aβ1-42 and Aβp3-42 Amyloid Beta Peptides: A SANS Study

Giulia Festa, Francesco Mallamace, Giulia Maria Sancesario, Carmelo Corsaro, Domenico Mallamace, Enza Fazio, Laura Arcidiacono, Victoria Garcia Sakai, Roberto Senesi, Enrico Preziosi, Giuseppe Sancesario, Carla Andreani

Research output: Contribution to journalArticlepeer-review


Aggregation states of amyloid beta peptides for amyloid beta A β 1 - 40 to A β 1 - 42 and A β p 3 - 42 are investigated through small angle neutron scattering (SANS). The knowledge of these small peptides and their aggregation state are of key importance for the comprehension of neurodegenerative diseases (e.g., Alzheimer's disease). The SANS technique allows to study the size and fractal nature of the monomers, oligomers and fibrils of the three different peptides. Results show that all the investigated peptides have monomers with a radius of gyration of the order of 10 Å, while the oligomers and fibrils display differences in size and aggregation ability, with A β p 3 - 42 showing larger oligomers. These properties are strictly related to the toxicity of the corresponding amyloid peptide and indeed to the development of the associated disease.

Original languageEnglish
JournalInternational Journal of Molecular Sciences
Issue number17
Publication statusPublished - Aug 24 2019


  • aggregation state
  • Alzheimer’s disease
  • beta amyloid
  • small angle neutron scattering

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry


Dive into the research topics of 'Aggregation States of Aβ<sub>1-40</sub>, Aβ<sub>1-42</sub> and Aβp<sub>3-42</sub> Amyloid Beta Peptides: A SANS Study'. Together they form a unique fingerprint.

Cite this