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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Litus EA,Kazakov AS,Sokolov AS,Nemashkalova EL,Galushko EI,Dzhus UF,Marchenkov VV,Galzitskaya OV,Permyakov EA,Permyakov SE

doi

10.1016/j.bbrc.2019.01.081

subject

Has Abstract

pub_date

2019-03-05 00:00:00

pages

248-253

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(19)30095-6

journal_volume

510

pub_type

杂志文章

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