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

Journal of biosciences

Georg Terstappen¹  Lia Millucci²  Davide Franceschini¹  Roberto Raggiaschi¹  Annalisa Santucci1² 

[1] SienaBiotech, via Fiorentina 1, 53100 Siena, Italy$$;Department of Molecular Biology, University of Siena$$

关键词: A𝛽(25-35);    aggregation;    amyloid;    assembly;    seeding;   

DOI  :  

来源: Indian Academy of Sciences

【 摘 要 】

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.

【 授权许可】

Unknown