RT Journal Article
T1 Amyloid capture and aggregation inhibition by human serum albumin
A1 Cora Calvo, Diego
A1 Al-Soufi, Wajih
A1 Novo, Mercedes
K1 Fluorescence
K1 Alzheimer's disease
K1 Amyloid
K1 Fluorescence correlation spectroscopy
K1 FCS
K1 Human serum albumin
K1 HSA
K1 Supramolecular association
K1 Aggregation
AB Alzheimer's disease (AD) is a prevalent neurodegenerative disorder characterized by amyloid-beta (Aβ) aggregation, primarily involving the peptides Aβ40 and Aβ42. Human serum albumin (HSA) has emerged as a potential therapeutic agent due to its ability to bind Aβ, inhibit aggregation, and promote disaggregation. This study quantitatively examined the interactions of HSA with both monomeric and aggregated forms of Aβ40 and Aβ42 using fluorescence techniques, including bulk steady-state fluorescence, fluorescence anisotropy, time-resolved fluorescence, and Fluorescence Correlation Spectroscopy (FCS). The binding constants determined from these methods were 4.45 × 104 M−1 for Aβ42 and 1.8 × 104 M−1 for Aβ40, indicating strong but differential affinities. FCS demonstrated that HSA effectively dissociates Aβ aggregates, shifting the equilibrium toward monomeric states, with the disaggregation capacity positively correlated with HSA concentration. These findings support HSA's utility in therapies like plasma exchange to reduce the cerebral Aβ burden, providing critical insights into its mechanistic role and therapeutic potential.
PB Elsevier
SN 0141-8130
YR 2025
FD 2025-04
LK https://hdl.handle.net/10347/43437
UL https://hdl.handle.net/10347/43437
LA eng
NO Cora, D., Al-Soufi, W., & Novo, M. (2025). Amyloid capture and aggregation inhibition by human serum albumin. International Journal of Biological Macromolecules, 301, 140367. 10.1016/j.ijbiomac.2025.140367
NO We thank the Spanish Ministerio de Ciencia e Innovación and the Xunta de Galicia for their financial support (PID2020-120378RB-I00, ED431B 2019/18). D.C. thanks the Xunta de Galicia for his research scholarship, “Campus de Especialización Campus Terra”. We thank Claus A.M. Seidel and Suren Felekyan for helpful discussions on the data treatment.
DS Minerva
RD 25 abr 2026