ArticleFEBS letters2026
Biophysical analysis of angiotensin II and amyloid-β cross-interaction in aggregation and membrane disruption.
Article in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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6 authors.
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Abstract
Amyloid-β (Aβ) aggregation is a hallmark of Alzheimer's disease. Endogenous peptides in the same environment may influence Aβ aggregation via direct interaction. This study explores the cross-interaction between Aβ and angiotensin II (AngII), a neuropeptide of the renin-angiotensin system, using biophysical assays and in silico modeling. Thioflavin T fluorescence, circular dichroism, and Congo Red assays show that AngII modestly reduces Aβ aggregation and membrane disruption in a dose-dependent manner. Liposome leakage assays confirm decreased membrane disruption. Modeling suggests AngII binds preferentially to disordered Aβ conformers. These findings indicate that AngII may modulate early amyloidogenic events and contribute to amyloid homeostasis, offering insights into the interplay between neuropeptides and amyloid pathology.
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