How pH Affects Amyloid Beta Peptide Self-Assembly
Author Information
Author(s): Xu Weixin, Zhang Ce, Derreumaux Philippe, Gräslund Astrid, Morozova-Roche Ludmilla, Mu Yuguang
Primary Institution: State Key Laboratory of Precision Spectroscopy, Institute of Theoretical and Computational Science, East China Normal University, Shanghai, China
Hypothesis
The study investigates how pH influences the self-assembly of amyloid beta peptides into fibrils.
Conclusion
The research shows that pH 5.0 is the most favorable condition for amyloid formation, while pH 8.4 significantly inhibits it.
Supporting Evidence
- At pH 5.0, the amyloid self-assembly proceeded rapidly, leading to a dense network of fibrils.
- At pH 2.9, amyloid fibrils were shorter and less abundant than at pH 5.0.
- At pH 8.4, amyloid formation was significantly depressed, with low fluorescence and unstructured aggregates observed.
Takeaway
This study found that changing the acidity of the environment can change how proteins stick together, which is important for understanding diseases like Alzheimer's.
Methodology
The study used molecular dynamics simulations and experimental techniques like ThT binding assays and atomic force microscopy to analyze the self-assembly of amyloid beta peptides at different pH levels.
Limitations
The study's findings may not fully represent the complex biological environment of the human brain.
Digital Object Identifier (DOI)
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