Interaction between human amphipathic apolipoproteins and amyloid β‐peptide: surface plasmon resonance studies

FEBS Letters

Shuvaev, Vladimir V.¹  Siest, Gérard¹ 

[1] Centre du Médicament, Université Henri Poincaré Nancy I, CNRS URA 597, 30 rue Lionnois, 54000 Nancy, France

关键词: Alzheimer's disease;    Amyloid beta-protein;    Apolipoprotein E;    Apolipoprotein A-I;    Apolipoprotein A-II;    Protein binding;    Apo;    apolipoprotein(s);    AD;    Alzheimer's disease;    Aβ;    amyloid β-peptide;    SPR;    surface plasmon resonance;    K D;    equilibrium dissociation constant;    k diss;    k ass;    rate constants of dissociation and association;    respectively;    RU;    refractive units;   

DOI  :  10.1016/0014-5793(96)00206-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown