2026-04-13T07:24:14Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/1921262025-12-05T14:11:40Zcom_2072_1057col_2072_478815col_2072_478917col_2072_478924col_2072_478933

00925njm 22002777a 4500 dc Alvarez-Berbel, Irene author Espargaró Colomé, Alba author Viayna, Elisabet author Caballero Hernández, Ana Belén author Busquets i Viñas, Ma. Antonia author Gámez Enamorado, Patrick author Luque Garriga, F. Xavier author Sabaté Lagunas, Raimon author 2023-01-12T11:25:57Z 2023-01-12T11:25:57Z 2022-10-30 2023-01-12T11:25:57Z One of the pathological hallmarks of Alzheimer's disease (AD) is the formation of amyloid-β plaques. Since acetylcholinesterase (AChE) promotes the formation of such plaques, the inhibition of this enzyme could slow down the progression of amyloid-β aggregation, hence being complementary to the palliative treatment of cholinergic decline. Anti-aggregation assays performed for apigenin and quercetin, which are polyphenolic compounds that exhibit inhibitory properties against the formation of amyloid plaques, reveal distinct inhibitory effects of these compounds on Aβ40 aggregation in the presence and absence of AChE. Furthermore, the analysis of the amyloid fibers formed in the presence of these flavonoids suggests that the Aβ40 aggregates present different quaternary structures, viz., smaller molecular assemblies are generated. In agreement with a non-competitive inhibition of AChE, molecular modeling studies indicate that these effects may be due to the binding of apigenin and quercetin at the peripheral binding site of AChE. Since apigenin and quercetin can also reduce the generation of reactive oxygen species, the data achieved suggest that multitarget catechol-type compounds may be used for the simultaneous treatment of various biological hallmarks of AD. Malaltia d'Alzheimer Pèptids Amiloïdosi Alzheimer's disease Peptides Amyloidosis Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction