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Journal of Biosciences

, Volume 34, Issue 2, pp 293–303 | Cite as

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

  • Lia Millucci
  • Roberto Raggiaschi
  • Davide Franceschini
  • Georg Terstappen
  • Annalisa Santucci
Article

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.

Keywords

Aβ(25–35) aggregation amyloid assembly seeding 

Abbreviations used

AD

Alzheimer disease

DMSO

dimethyl sulphoxide

HFIP

hexafluorisopropanol

IBM

inclusion body myositis

NCC

nucleated conformational conversion’

OD

optical density

PBS

phosphate buffered saline

pI

isoelectric point

SDS

sodium dodecyl sulphate

TFA

trifluoroacetic acid

Th-T

thioflavin-T

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Copyright information

© Indian Academy of Sciences 2009

Authors and Affiliations

  • Lia Millucci
    • 1
  • Roberto Raggiaschi
    • 2
  • Davide Franceschini
    • 2
  • Georg Terstappen
    • 2
  • Annalisa Santucci
    • 1
  1. 1.Department of Molecular BiologyUniversity of SienaSienaItaly
  2. 2.SienaBiotechSienaItaly

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