REVIEW article
Front. Mol. Biosci.
Sec. Molecular Biophysics
Volume 12 - 2025 | doi: 10.3389/fmolb.2025.1704653
This article is part of the Research TopicBiophysical Insights into the Molecular Mechanisms of NeurodegenerationView all 3 articles
Biophysical insights into the molecular mechanisms of beta amyloid aggregation and its toxic effects in Alzheimer's disease
Provisionally accepted
- 1Kermanshah University of Medical Sciences, Kermanshah, Iran
- 2Sapienza University, Rome, Italy
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Alzheimer's disease is recognized as the most common neurodegenerative disorder, characterized by the presence of amyloid plaques, which have consistently garnered significant attention. Since the disease was first identified, extensive research has been devoted to investigating these plaques. As our understanding of the disease has progressed, the detrimental role of plaques has been questioned, leading to the hypothesis that amyloid oligomeric aggregates are the main culprits. Nevertheless, subsequent research indicated that the concentrations of amyloids employed in the experiments were considerably elevated compared to physiological conditions, and that at physiological concentrations, amyloids do not exhibit significant accumulation or toxicity. This article aims to offer a detailed biophysical perspective on the formation of amyloid aggregates under physiological conditions and their impact on membranes, providing valuable insights for researchers in this field.
Keywords: Alzheimer's disease, amyloid aggregation, Molecular mechanisms, Membranes, damage, Copper, Cholesterol, oxidized
Received: 13 Sep 2025; Accepted: 16 Oct 2025.
Copyright: © 2025 Bagheri and Saso. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Luciano Saso, luciano.saso@uniroma1.it
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