| Autor: |
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 |
| Jazyk: |
angličtina |
| Rok vydání: |
2019 |
| Předmět: |
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| Zdroj: |
International Journal of Molecular Sciences, Vol 20, Iss 17, p 4126 (2019) |
| Druh dokumentu: |
article |
| ISSN: |
1422-0067 |
| DOI: |
10.3390/ijms20174126 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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