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Amyloid β Peptide Modifies Membrane Architecture and Surface Electrostatic Properties of Human Red Blood Cells
Galya Staneva1,2, Vesela Yordanova1,2, Avgustina Danailova1
1Institute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, "Acad. G. Bonchev" Str., Block 21, 1113 Sofia, Bulgaria.
Abstract:
Abnormal accumulation of amyloid-beta (Aβ) peptides in the brain is a hallmark of Alzheimer's disease (AD). Importantly, the peripheral blood cells are also exposed to the effects of pathological peptides that accumulate in AD. Herein, the interaction of Aβ42 oligomers (Aβ42) with human red blood cells (RBCs) and erythrocyte ghosts as in vitro models for AD is studied combining fluorescence spectroscopy, fluorescence microscopy, and electrokinetics. The binding of Aβ42 to RBCs was evidenced by the use of a fluorescent-labeled peptide. The membrane lipid order increased with the increase in both the Aβ42 concentration and the incubation time, creating a lipid-protein microenvironment characterized by higher molecular order and reduced heterogeneity in RBC membranes compared to control conditions. Notably, the increase in lipid order was less pronounced in erythrocyte ghosts than in intact RBCs. Furthermore, the ζ-potential measurements revealed Aβ42 induced alteration of the surface potential of RBCs in a concentration- and time-dependent manner, with freshly isolated RBCs exhibiting a highly negative potential that became increasingly negative at higher Aβ42 concentrations. These findings suggest that Aβ42 not only impacts neuronal function but also significantly alters the physical properties of RBCs that might compromise their function, potentially contributing to the systemic effects observed in AD.
Insights
Alzheimer's disease (AD) involves amyloid-beta (Aβ) affecting brain cells. This study shows Aβ42 also alters red blood cell (RBC) physical properties, potentially impacting systemic AD effects.
Area of Science:
- Neuroscience
- Biochemistry
- Cell Biology
Background:
- Alzheimer's disease (AD) is characterized by amyloid-beta (Aβ) accumulation in the brain.
- Peripheral blood cells, including red blood cells (RBCs), are also exposed to Aβ.
- Understanding Aβ interactions with non-neuronal cells like RBCs is crucial for comprehending AD's systemic impact.
Purpose of the Study:
- To investigate the interaction between amyloid-beta 42 (Aβ42) oligomers and human red blood cells (RBCs) as an in vitro model for Alzheimer's disease.
- To analyze the effects of Aβ42 on RBC membrane physical properties, including lipid order and surface potential.
- To compare the effects of Aβ42 on intact RBCs versus erythrocyte ghosts.
Main Methods:
- Fluorescence spectroscopy and microscopy were used to visualize and quantify Aβ42 binding to RBCs.
- Changes in RBC membrane lipid order were assessed.
- Electrokinetic measurements (ζ-potential) were employed to evaluate alterations in RBC surface charge.
Main Results:
- Fluorescently labeled Aβ42 demonstrated binding to RBCs.
- Aβ42 increased RBC membrane lipid order in a concentration- and time-dependent manner.
- Aβ42 significantly altered the surface potential (ζ-potential) of RBCs, making it more negative.
Conclusions:
- Amyloid-beta 42 (Aβ42) significantly alters the physical properties of red blood cells (RBCs).
- These alterations in RBCs, including increased lipid order and modified surface potential, may compromise their function.
- The findings suggest Aβ42's impact extends beyond the brain, potentially contributing to systemic effects in Alzheimer's disease.
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