In vitro perturbation of aggregation processes in β-amyloid peptides: A spectroscopic study

被引：34

作者：

Sgarbossa, Antonella ^{[1
]}

Buselli, Dario ^{[1
]}

Lenci, Francesco ^{[1
]}

机构：

[1] CNR, Ist Biofis, Unita Pisa, I-56100 Pisa, Italy

来源：

FEBS LETTERS | 2008年 / 582卷 / 23-24期

关键词：

Alzheimer; beta-Amyloid; Hypericin; Neurotoxic peptide; Intermolecular interaction;

D O I：

10.1016/j.febslet.2008.08.039

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have performed an in vitro study to investigate the molecular basis of the aggregation kinetic of 1-40 beta-amyloid peptides (Ab and the possibility of affecting this aggregation process using an exogenous natural polycyclic pigment, hypericin (Hyp). The effect of Hyp on the self-assembly process at different times of the aggregation kinetic has been investigated utilizing a chaperon-like molecule, alpha-crystallin. Circular dichroism and fluorescence results suggest that Hyp can associate to precursors of the mature fibrils and perturb the aggregation process through intermolecular interactions with the Ab peptides.

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页码：3288 / 3292

页数：5

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