A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid beta aggregation.
We present the first electrochemical detection, characterization, and kinetic study of the aggregation of Alzheimer's disease (AD) amyloid beta peptides (Abeta-40, Abeta-42) using three different voltammetric techniques at a glassy carbon electrode (GCE). This method is based on detecting changes in the oxidation signal of tyrosine (Tyr) residue. As the peptides aggregate, there are structure conformational changes, which affect the degree of exposure of Tyr to the molecular surface of the peptides. The results show significant differences in the aggregation process between the two peptides, and these correlate highly with established techniques. The method is rapid and label-free, and the principle can be universally applied to other protein aggregation studies related to diseases, such as Huntington's, Parkinson's, and Creutzfeldt Jacob (CJD). This method could also be explored in screening for the effectiveness of AD therapies.
Vestergaard
Mun'delanji
M
Department of Biological Science and Biotechnology, School of Material Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Nomi City, Ishikawa 923-1292, Japan. munde@jaist.ac.jp
Kerman
Kagan
K
Saito
Masato
M
Nagatani
Naoki
N
Takamura
Yuzuru
Y
Tamiya
Eiichi
E
D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D004563:Electrochemistry; D007700:Kinetics; D018625:Microscopy, Atomic Force; D010446:Peptide Fragments / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism*
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments