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Electrochemical Detection of Isoform‐Specific Interaction between Apolipoprotein E and Amyloid‐β
Author(s) -
Su Han,
Jin Yiyun,
Noroozifar Meissam,
Kerman Kagan
Publication year - 2019
Publication title -
chemelectrochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.182
H-Index - 59
ISSN - 2196-0216
DOI - 10.1002/celc.201800985
Subject(s) - apolipoprotein e , gene isoform , chemistry , surface plasmon resonance , cyclic voltammetry , amyloid (mycology) , amyloid precursor protein , biophysics , apolipoprotein b , peptide , biochemistry , alzheimer's disease , cholesterol , electrochemistry , medicine , nanotechnology , biology , materials science , disease , nanoparticle , gene , inorganic chemistry , electrode
Alzheimer's disease (AD) is characterized by the formation of neurofibrillary tangles (NFTs) including amyloid‐β (Aβ) in the brain. Apolipoprotein E (ApoE) plays a key role in the homeostasis of cholesterol and other lipids in blood circulation. The interaction between ApoE and Aβ has been implicated in the pathological progression of AD. In this study, the interaction of three isoforms of ApoE4, ApoE3 and ApoE2 with Aβ 1–40 and Aβ 1–42 peptides was investigated using cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). Interactions between Aβ peptides and ApoE isoforms were determined by monitoring the changes in ΔR ct of Nyquist plots. The affinity between Aβ 1–40 and Aβ 1–42 and ApoE isoforms interpreted from EIS data followed the trend: ApoE4>ApoE3>ApoE2. Using surface plasmon resonance (SPR), the binding affinity (K D ) constants for the interaction of ApoE4 with Aβ 1–40 and Aβ 1–42 peptides were determined as 185±21 nM and 156±18 nM, respectively, in agreement with our electrochemical results. Our proof‐of‐principle study demonstrates that EIS provides a promising platform for the investigation of protein‐protein interactions implicated in AD.