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 (A?) peptide into insoluble fibrils. In the present work we study the A?1-40 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 A?1-40 peptide has a good aggregation capability but can also adopt an unfolded conformation in particular conditions, as for example, when incubated in DMSO.
SANS study of Amyloid ?1-40 : Unfolded monomers in DMSO, multidimensional aggregates in water medium
Longo Sveva;
2019
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 (A?) peptide into insoluble fibrils. In the present work we study the A?1-40 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 A?1-40 peptide has a good aggregation capability but can also adopt an unfolded conformation in particular conditions, as for example, when incubated in DMSO.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
