Interaction between human amphipathic apolipoproteins and amyloid beta-peptide: surface plasmon resonance studies.
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.
Shuvaev
V V
VV
Centre du Médicament, Université Henri Poincaré Nancy, France.
Siest
G
G
D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism*; D016632:Apolipoprotein A-I / Q000378:metabolism*; D016633:Apolipoprotein A-II / Q000378:metabolism*; D053318:Apolipoprotein E3; D001057:Apolipoproteins E / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D012965:Sodium Chloride / Q000494:pharmacology
D016229:Amyloid beta-Peptides; D016632:Apolipoprotein A-I; D016633:Apolipoprotein A-II; D053318:Apolipoprotein E3; D001057:Apolipoproteins E; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); D012965:Sodium Chloride