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

被引：65

作者：

Millucci, Lia ^{[1
]}

Raggiaschi, Roberto ^{[2
]}

Franceschini, Davide ^{[2
]}

Terstappen, Georg ^{[2
]}

Santucci, Annalisa ^{[1
]}

机构：

[1] Univ Siena, Dept Mol Biol, I-53100 Siena, Italy

[2] SienaBiotech, I-53100 Siena, Italy

来源：

JOURNAL OF BIOSCIENCES | 2009年 / 34卷 / 02期

关键词：

A beta(25-35); aggregation; amyloid; assembly; seeding; AMYLOID FIBRIL FORMATION; PROTEIN; NEURODEGENERATION; CONVERSION; TOXICITY; STATE; PH;

D O I：

10.1007/s12038-009-0033-3

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The highly toxic A beta(25-35) is a peculiar peptide that differs from all the other commonly studied beta-amyloid peptides because of its extremely rapid aggregation properties and enhanced neurotoxicity. We investigated A beta(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 A beta(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 A beta(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.

引用

页码：293 / 303

页数：11

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