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 journalArticle

Abstract

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
Volume20
Issue number17
DOIs
Publication statusPublished - Aug 24 2019

Fingerprint

Small Angle Scattering
Neutrons
Neutron scattering
Amyloid
Peptides
peptides
neutron scattering
Agglomeration
Oligomers
oligomers
Monomers
Neurodegenerative diseases
Fractals
monomers
Aptitude
Amyloid beta-Peptides
Neurodegenerative Diseases
gyration
Toxicity
Alzheimer Disease

Keywords

  • 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

Cite this

Festa, G., Mallamace, F., Sancesario, G. M., Corsaro, C., Mallamace, D., Fazio, E., ... Andreani, C. (2019). Aggregation States of Aβ1-40, Aβ1-42 and Aβp3-42 Amyloid Beta Peptides: A SANS Study. International Journal of Molecular Sciences, 20(17). https://doi.org/10.3390/ijms20174126

Aggregation States of Aβ1-40, Aβ1-42 and Aβp3-42 Amyloid Beta Peptides : A SANS Study. / Festa, Giulia; Mallamace, Francesco; Sancesario, Giulia Maria; Corsaro, Carmelo; Mallamace, Domenico; Fazio, Enza; Arcidiacono, Laura; Garcia Sakai, Victoria; Senesi, Roberto; Preziosi, Enrico; Sancesario, Giuseppe; Andreani, Carla.

In: International Journal of Molecular Sciences, Vol. 20, No. 17, 24.08.2019.

Research output: Contribution to journalArticle

Festa, G, Mallamace, F, Sancesario, GM, Corsaro, C, Mallamace, D, Fazio, E, Arcidiacono, L, Garcia Sakai, V, Senesi, R, Preziosi, E, Sancesario, G & Andreani, C 2019, 'Aggregation States of Aβ1-40, Aβ1-42 and Aβp3-42 Amyloid Beta Peptides: A SANS Study', International Journal of Molecular Sciences, vol. 20, no. 17. https://doi.org/10.3390/ijms20174126
Festa, Giulia ; Mallamace, Francesco ; Sancesario, Giulia Maria ; Corsaro, Carmelo ; Mallamace, Domenico ; Fazio, Enza ; Arcidiacono, Laura ; Garcia Sakai, Victoria ; Senesi, Roberto ; Preziosi, Enrico ; Sancesario, Giuseppe ; Andreani, Carla. / Aggregation States of Aβ1-40, Aβ1-42 and Aβp3-42 Amyloid Beta Peptides : A SANS Study. In: International Journal of Molecular Sciences. 2019 ; Vol. 20, No. 17.
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