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The binding of monomeric amyloid β peptide to serum albumin is affected by major plasma unsaturated fatty acids

Litus, E.A., Kazakov, A.S., Sokolov, A.S., Nemashkalova, E.L., Galushko, E.I., Dzhus, U.F., Marchenkov, V.V., Galzitskaya, O.V., Permyakov, E.A., Permyakov, S.E.
Biochemical and biophysical research communications 2019 v.510 no.2 pp. 248-253
Alzheimer disease, amyloid, arachidonic acid, copper, dissociation, human serum albumin, linoleic acid, spectroscopy, surface plasmon resonance
Human serum albumin (HSA) serves as a natural depot of amyloid β peptide (Aβ). Improvement of Aβ binding to HSA should impede Alzheimer's disease (AD). We developed a method for quantitation of the interaction between monomeric Aβ40/42 and HSA using surface plasmon resonance spectroscopy. The dissociation constant of HSA complex with recombinant Aβ40/42 is 0.2–0.3 μM. Flemish variant of Aβ40 has 2.5–10-fold higher affinity to HSA. The parameters of the HSA-Aβ interaction are selectively sensitive to HSA binding of major plasma unsaturated fatty acids and Cu2+. Linoleic and arachidonic acids promote the HSA-Aβ42 interaction. The developed methodology for quantitation of HSA-Aβ interaction may serve as a tool for search of compounds favoring HSA-Aβ interaction, thereby preventing AD progression.