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    • Keywords


      A𝛽(25-35); aggregation; amyloid; assembly; seeding

    • 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 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.

    • Author Affiliations


      Lia Millucci1 Roberto Raggiaschi2 Davide Franceschini2 Georg Terstappen2 Annalisa Santucci1

      1. Department of Molecular Biology, University of Siena
      2. SienaBiotech, via Fiorentina 1, 53100 Siena, Italy
    • Dates

  • Journal of Biosciences | News

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      Posted on July 25, 2019

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