Abstract
The membrane roughness of Neuro-2a neroblastoma cells is measured by using noninterferometric wide-field optical profilometry. The cells are treated with the fibril and oligomer conformers of amyloid-beta (Aβ) 42, which is a peptide of 42 amino acids related to the development of Alzheimer's disease. We find that both the Aβ42 fibrils and Aβ42 oligomers reduced the cell membrane roughness, but the effect of Aβ42 oligomers was faster and stronger than that of the fibrils. We also apply direct-current electric field (dcEF) stimulations on the cells. A dcEF of 300 mV/mm can increase the membrane roughness under the treatment of Aβ42. These results suggest that Aβ42 can decrease the membrane compliance of live neuroblastoma cells, and dcEFs may counteract this effect.
Highlights
Alzheimer’s disease (AD) is a progressive neurodegenerative disease in which one of the defining characteristics is global cognitive decline including memory,[1] orientation, judgment, and reasoning
Because the height variations on the whole cell are often larger than the noninterferometric widefield optical profilometry (NIWOP) measurement dynamic range, we arbitrarily selected a 10 μm × 10 μm region at the edge of each cell, and calculated the standard deviations of the membrane height in this region as the estimation of membrane roughness
We demonstrated that high-sensitivity optical profilometry was useful for the diagnosis of cellular effects of Aβ42 peptides and direct-current electric field (dcEF)
Summary
Alzheimer’s disease (AD) is a progressive neurodegenerative disease in which one of the defining characteristics is global cognitive decline including memory,[1] orientation, judgment, and reasoning. Amyloid-beta 42 (Aβ42) is a peptide composed of 42 amino acids that is believed to be related to the development of AD.[2] Aβ peptides can bind to various biomolecules, such as proteins, lipids, and proteoglycans, and cause toxic effects to neurons by perturbing the properties and functions of plasma membranes.[3,4,5] The Aβ peptides can assemble into various degrees of polymerization, and the conformations of oligomers, proto-fibrils, and fibrils are found to exist in brain lesions of AD patients. We may conjecture that the Aβ peptides have the ability to vary other mechanical characteristics of cell membranes
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