Aggregation states of amyloid beta peptides for amyloid beta A beta(1-40) to A beta(1-42) and A beta 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 angstrom, while the oligomers and fibrils display differences in size and aggregation ability, with A beta 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.

Festa, G., Mallamace, F., Sancesario, G.m., Corsaro, C., Mallamace, D., Fazio, E., et al. (2019). Aggregation states of Aβ1-40, Aβ1-42 and Aβp3-42 amyloid beta peptides: A SANS study. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 20(17), 4126 [10.3390/ijms20174126].

Aggregation states of Aβ1-40, Aβ1-42 and Aβp3-42 amyloid beta peptides: A SANS study

Festa G.;Corsaro C.;Senesi R.;Preziosi E.;Andreani C.
2019

Abstract

Aggregation states of amyloid beta peptides for amyloid beta A beta(1-40) to A beta(1-42) and A beta 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 angstrom, while the oligomers and fibrils display differences in size and aggregation ability, with A beta 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.
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin)
English
Alzheimer’s disease; aggregation state; beta amyloid; small angle neutron scattering
Festa, G., Mallamace, F., Sancesario, G.m., Corsaro, C., Mallamace, D., Fazio, E., et al. (2019). Aggregation states of Aβ1-40, Aβ1-42 and Aβp3-42 amyloid beta peptides: A SANS study. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 20(17), 4126 [10.3390/ijms20174126].
Festa, G; Mallamace, F; Sancesario, Gm; Corsaro, C; Mallamace, D; Fazio, E; Arcidiacono, L; Sakai, Vg; Senesi, R; Preziosi, E; Sancesario, G; Andreani, C
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/224789
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