RT Book,_Section
T1 Early aggregation of amyloid-β(1–42) studied by fluorescence correlation spectroscopy
A1 Novo, Mercedes
A1 Pérez González, Cibrán
A1 Freire Leira, María Sonia
A1 Al-Soufi, Wajih
K1 FCS
K1 Amyloid-b
K1 Single-molecule fluorescence
AB Alzheimer's disease (AD) is a progressive neurodegenerative disease affecting cognitive and memory abilities and is believed to be linked to the formation and accumulation of neurotoxic aggregates of the Amyloid-P peptide (Aj3). In particular, it is the formation of soluble pre-fibrillar oligomers within the earlystage of Aj3 aggregation which is thought to representa key step in the development of AD, thus underlining the interest in characterizing the aggregation process and the nature of these aggregates. In this context, fluorescence correlation spectroscopy (FCS) has emerged as a valuable alternative for the study ofthese systems in solution. lndeed, the use ofFCS to study terminally labelled Aj3 provides a means to detect changes in the size and concentration of initially monomeric Aj3 samples by monitoring these fluorescently labelled species fi:eely diffusing in solution with single-molecule resolution. Herein, we show how tocmploy FCS to study the early aggregation process of AP(l-42) and how this can be used to estimate the critica! concentration for oligomer formation and to characterize the aggregates formed.
PB Humana Press
SN 978-1-0716-2596-5
YR 2023
FD 2023
LK https://hdl.handle.net/10347/39304
UL https://hdl.handle.net/10347/39304
LA eng
NO Novo Rodríguez, M. de la M., Pérez-González, C., Freire Leira, M. S., & Al-Soufi, W. (2023). Early aggregation of amyloid-β (1-42) studied by fluorescence correlation spectroscopy. In Protein aggregation. (1-14). Humana Press
NO Dixitalización da versión impresa do capítulo do libro "Protein aggregation" publicado en 2023
DS Minerva
RD 24 abr 2026