Rapid aggregation and assembly in aqueous solution of Aβ (25-35) peptide.
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Date
2009-06
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Abstract
The highly toxic Aβ(25-35) is a peculiar peptide that differs from all the other commonly studied β-amyloid peptides
because of its extremely rapid aggregation properties and enhanced neurotoxicity. We investigated Aβ(25-35)
aggregation in H
2
O at pH 3.0 and at pH 7.4 by means of in-solution analyses. Adopting UV spectroscopy, Congo
red spectrophotometry and thiofl avin T fl uorimetry, we were able to quantify, in water, the very fast assembling time
necessary for Aβ(25-35) to form stable insoluble aggregates and their ability to seed or not seed fi bril growth. Our
quantitative results, which confi rm a very rapid assembly leading to stable insoluble aggregates of Aβ(25-35) only
when incubated at pH 7.4, might be helpful for designing novel aggregation inhibitors and to shed light on the in vivo
environment in which fi bril formation takes place.
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Millucci Lia, Raggiaschi Roberto, Franceschini Davide, Terstappen Georg, Santucci Annalisa. Rapid aggregation and assembly in aqueous solution of Aβ (25-35) peptide. Journal of Biosciences. 2009 Jun; 34(2): 293-303.