Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5656
Title: Rapid aggregation and assembly in aqueous solution of A beta (25-35) peptide
Authors: Millucci, Lia 
Raggiaschi, R
Franceschini, D
Terstappen, G
Santucci, Annalisa 
Issue Date: 2009
Project: None 
Journal: JOURNAL OF BIOSCIENCES
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.
Description: 
24579
URI: http://hdl.handle.net/20.500.12779/5656
ISSN: 0250-5991
DOI: 10.1007/s12038-009-0033-3
Appears in Collections:Publications

Show full item record

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.