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 H2O 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.

Millucci, L., Raggiaschi, R., Franceschini, D., Terstappen, G., & Santucci, A. (2009). Rapid aggregation and assembly in aqueous solution of A beta (25-35) peptide. JOURNAL OF BIOSCIENCES, 34(2), 293-303 [10.1007/s12038-009-0033-3].

Rapid aggregation and assembly in aqueous solution of A beta (25-35) peptide

MILLUCCI, LIA;SANTUCCI, ANNALISA
2009

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 H2O 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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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/20897
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