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

doi:10.1016/j.physa.2018.11.027

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 journal › Article › peer-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 language	English
Pages (from-to)	385-391
Number of pages	7
Journal	Physica A: Statistical Mechanics and its Applications
Volume	517
DOIs	https://doi.org/10.1016/j.physa.2018.11.027
Publication status	Published - Mar 1 2019

Keywords

Amyloid aggregation
Amyloid fibrils
SANS

ASJC Scopus subject areas

Statistics and Probability
Condensed Matter Physics

Access to Document

10.1016/j.physa.2018.11.027

Cite this

Festa, G., Sancesario, G., Corsaro, C., Longo, S., Mallamace, D., Fazio, E., Arcidiacono, L., Sakai, V. G., Senesi, R., Sancesario, G., Mallamace, F., & Andreani, C. (2019). SANS study of Amyloid β ₁₋₄₀: Unfolded monomers in DMSO, multidimensional aggregates in water medium. Physica A: Statistical Mechanics and its Applications, 517, 385-391. https://doi.org/10.1016/j.physa.2018.11.027

Festa, G, Sancesario, G, Corsaro, C, Longo, S, Mallamace, D, Fazio, E, Arcidiacono, L, Sakai, VG, Senesi, R, Sancesario, G, Mallamace, F & Andreani, C 2019, 'SANS study of Amyloid β ₁₋₄₀: Unfolded monomers in DMSO, multidimensional aggregates in water medium', Physica A: Statistical Mechanics and its Applications, vol. 517, pp. 385-391. https://doi.org/10.1016/j.physa.2018.11.027

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AU - Corsaro, Carmelo

AU - Longo, Sveva

AU - Mallamace, Domenico

AU - Fazio, Enza

AU - Arcidiacono, Laura

AU - Sakai, Victoria Garcia

AU - Senesi, Roberto

AU - Sancesario, Giulia

AU - Mallamace, Francesco

AU - Andreani, Carla

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