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

Author:
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.
Source:
Biochemical and biophysical research communications 2019 v.510 no.2 pp. 248-253
ISSN:
0006-291X
Subject:
Alzheimer disease, amyloid, arachidonic acid, copper, dissociation, human serum albumin, linoleic acid, spectroscopy, surface plasmon resonance
Abstract:
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.
Agid:
6280687