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Interaction between human amphipathic apolipoproteins and amyloid β‐peptide: surface plasmon resonance studies
Author(s) -
Shuvaev Vladimir V.,
Siest Gérard
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00206-2
Subject(s) - peptide , surface plasmon resonance , chemistry , amyloid (mycology) , dissociation constant , senile plaques , biophysics , amphiphile , biochemistry , apolipoprotein e , p3 peptide , population , alzheimer's disease , amyloid precursor protein , medicine , biology , receptor , nanotechnology , nanoparticle , organic chemistry , materials science , disease , inorganic chemistry , environmental health , copolymer , polymer
Several apolipoproteins including apoE and apoA‐I are known to be associated with amyloid β‐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 β‐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 β‐peptide. On the other hand, only a small population of synthetic amyloid β‐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 β‐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 β‐peptide was suggested.