Interaction between human amphipathic apolipoproteins and amyloid beta-peptide: surface plasmon resonance studies.

Abstract:

:Several apolipoproteins including apoE and apoA-I are known to be associated with amyloid beta-peptide, a major component of senile plaques in Alzheimer's disease. In the present study the interaction between three human amphipathic apolipoproteins apoE3, apoA-I and apoA-II and immobilized amyloid beta-peptide (1-40) was quantified by plasmon resonance. The interactions were saturable and reversible. The results demonstrated a high affinity of the binding of amphipathic apolipoproteins to amyloid beta-peptide. On the other hand, only a small population of synthetic amyloid beta-peptide participated in the interaction. The apparent equilibrium dissociation constants K(D) were 10 nM for apoE3, 25 nM for apoA-I and 80 nM for apoA-II under physiological conditions. The affinity of the apoE3-amyloid beta-peptide binding was not affected by pH in the range 6.0-8.0 but was significantly increased by high salt concentration. ApoA-I mainly followed similar patterns. A major participation of hydrophobic forces in the binding of apoE3 and apoA-I to amyloid beta-peptide was suggested.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Shuvaev VV,Siest G

doi

10.1016/0014-5793(96)00206-2

subject

Has Abstract

pub_date

1996-03-25 00:00:00

pages

9-12

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)00206-2

journal_volume

383

pub_type

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