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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 23, Number 12
BKCSDE 23(12)
December 20, 2002

Title	Protectors of Oxidative Stress Inhibit Aβ (1-42) Aggregation in vitro
Author	Byungmun Kong, Jeonghoon Ueom, Inkyung Kim, Dongyeol Lim, Jongmin Kang, Kyunghee Lee
Keywords	Hsp104, Antioxidants, Curcumin, A b aggregation
Abstract	Reactive oxygen species (ROS) have been investigated to have pivotal roles on amyloidogenecity of β-amyloid peptide (Aβ), the major component of senile plaques in Alzheimer's disease (AD) brain. Addition of radical scavengers is one of the on-going strategies for therapeutic treatment for AD patients. Hsp104 protein including two ATP binding sites from Saccharomyces cerevisiae, as a molecular chaperone, was known to function as a protector of ROS generation when exposed to oxidative stress in our previous study. This observation has led us to investigate Hsp104 protein as a molecular mediator of Aβ aggregation in this study. We have developed a new way of expression for Hsp104 protein using GST-fusion tag. As we expected, formation of A b aggregate was protected by wild type Hsp104 protein, but not by the two ATP-binding site mutant, based on Thioflavin-T fluorescence. Interestingly, Hsp104 protein was observed to keep Aβfrom forming aggregates independent of ATP binding. On the other hand, disaggregation of Aβ aggregates by wild type Hsp104 was totally dependent on the presence of ATP. On the other hand, mutant Hsp104 with two ATP binding sites altered exhibited no inhibition. Another effective antioxidant, hydrazine analogs of curcumin were also effective in Aβ fibrilization as protectors against oxidative stress. Based on these observations we conclude that Hsp104 and curcumin derivatives, as protectors of oxidative stress, inhibit Aβaggregation in vitro and can be candidates for therapeutic approaches in cure of some neurodegenerative diseases.
Page	1773 - 1777
Full Text	PDF

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