• Georg Terstappen

      Articles written in Journal of Biosciences

    • Rapid aggregation and assembly in aqueous solution of A𝛽 (25-35) peptide

      Lia Millucci Roberto Raggiaschi Davide Franceschini Georg Terstappen Annalisa Santucci

      More Details Abstract Fulltext PDF

      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 thioflavin T fluorimetry, 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 fibril growth. Our quantitative results, which confirm 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 fibril formation takes place.

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