Document Type
Article
Publication Date
2022
Keywords
Alzheimer’s Disease, Amyloid-β Peptide, Human Serum Albumin, Ibuprofen, Surface Plasmon Resonance, Aβ Fibrillation, Electron Microscopy, Molecular Docking
Digital Object Identifier (DOI)
https://doi.org/10.3390/ijms23116168
Abstract
The deposition of amyloid-β peptide (Aβ) in the brain is a critical event in the progression of Alzheimer’s disease (AD). This Aβ deposition could be prevented by directed enhancement of Aβ binding to its natural depot, human serum albumin (HSA). Previously, we revealed that specific endogenous ligands of HSA improve its affinity to monomeric Aβ. We show here that an exogenous HSA ligand, ibuprofen (IBU), exerts the analogous effect. Plasmon resonance spectroscopy data evidence that a therapeutic IBU level increases HSA affinity to monomeric Aβ40/Aβ42 by a factor of 3–5. Using thioflavin T fluorescence assay and transmission electron microcopy, we show that IBU favors the suppression of Aβ40 fibrillation by HSA. Molecular docking data indicate partial overlap between the IBU/Aβ40-binding sites of HSA. The revealed enhancement of the HSA–Aβ interaction by IBU and the strengthened inhibition of Aβ fibrillation by HSA in the presence of IBU could contribute to the neuroprotective effects of the latter, previously observed in mouse and human studies of AD.
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
International Journal of Molecular Sciences, v. 23, issue 11, art. 6168
Scholar Commons Citation
Litus, Ekaterina A.; Kazakov, Alexei S.; Deryusheva, Eugenia I.; Nemashkalova, Ekaterina L.; Shevelyova, Marina P.; Machulin, Andrey V.; Nazipova, Aliya A.; Permyakova, Maria E.; Uversky, Vladimir N.; and Permyakov, Sergei E., "Ibuprofen Favors Binding of Amyloid-β Peptide to Its Depot, Serum Albumin" (2022). Molecular Medicine Faculty Publications. 937.
https://digitalcommons.usf.edu/mme_facpub/937
