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Detection of β-Amyloid Peptide Aggregation Using DNA Electrophoresis

✍ Scribed by Bong Whan Ahn; Dong Up Song; Young Do Jung; Kee Oh Chay; Min A Chung; Sung Yeul Yang; Boo Ahn Shin

Publisher
Elsevier Science
Year
2000
Tongue
English
Weight
188 KB
Volume
284
Category
Article
ISSN
0003-2697

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✦ Synopsis

DNA could readily associate with the aggregated forms of the ␤-amyloid peptides ␤(1-40) and ␤(25-35), giving rise to a shift in the electrophoretic mobility of DNA. As a result, DNA was retained at the top of a 1% agarose gel. In contrast, the electrophoretic mobility of DNA was little influenced by the monomeric forms of ␤(1-40) and ␤(25-30). DNA from different sources such as phage, Escherichia coli plasmid, and human gene showed similar results. However, the electrophoretic mobility of RNA was shifted by the monomeric ␤(1-40) and ␤(25-35) as well as by the aggregated ␤(1-40) and ␤(25-35). The association of DNA with the aggregated ␤-amyloid peptides could occur at pH 4 -9. The inhibitory action of hemin on ␤-amyloid aggregation could be confirmed using the DNA mobility shift assay. These results indicate that the DNA mobility shift assay is useful for kinetic study of ␤-amyloid aggregation as well as for testing of agents that might modulate ␤-amyloid aggregation.

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