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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

The relationship between the aggregational state of the amyloid-beta peptides and free radical generation by the peptides.

In the present study, we investigated whether or not the amyloid-beta protein (Abeta) peptide itself spontaneously generates free radicals using electron spin resonance (ESR) spectroscopy while also monitoring the aggregational state of Abeta and Abeta-induced cytotoxicity. The present results demonstrated a four-line spectrum in the presence of both Abeta40 and Abeta42 with Ntert-butyl-alpha-phenylnitrone (PBN), but not in the presence of PBN alone in phosphate-buffered saline (PBS). The fact that the four-line spectrum obtained for the Abeta/PBN in PBS was completely abolished in the presence of the iron-chelating agent Desferal demonstrated the observed four-line spectrum to be iron-dependent. The present study also revealed that either Abeta40 or Abeta42 with PBN in phosphate buffer (PB) did not produce any definite four-line spectrum. Both a thioflavine-T (Th-T) fluorometric assay and circular dichroism (CD) spectroscopy showed the amyloid fibril formation of Abeta in PBS to be much higher than that of Abeta in PB. Moreover, Abeta-induced cytotoxicity assays showed Abeta incubated in PBS to be more cytotoxic than that incubated in PB. These results thus suggest that Abeta-associated free radical generation is strongly influenced by the aggregational state of the peptides.[1]

References

  1. The relationship between the aggregational state of the amyloid-beta peptides and free radical generation by the peptides. Monji, A., Utsumi, H., Ueda, T., Imoto, T., Yoshida, I., Hashioka, S., Tashiro , K., Tashiro, N. J. Neurochem. (2001) [Pubmed]
 
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