Unknown

Dataset Information

0

Effects of Congo red on a?(1-40) fibril formation process and morphology.


ABSTRACT: Alzheimer's disease (AD), an age-related neurodegenerative disorder, is the most common form of dementia, and the seventh-leading cause of death in the United States. Current treatments offer only symptomatic relief; thus, there is a great need for new treatments with disease-modifying potential. One pathological hallmark of AD is so-called senile plaques, mainly made up of ?-sheet-rich assemblies of 40- or 42-residue amyloid ?-peptides (A?). Hence, inhibition of A? aggregation is actively explored as an option to prevent or treat AD. Congo red (CR) has been widely used as a model antiamyloid agent to prevent A? aggregation. Herein, we report detailed morphological studies on the effect of CR as an antiamyloid agent, by circular dichroism spectroscopy, photo-induced cross-linking reactions, and atomic force microscopy. We also demonstrate the effect of CR on a preaggregated sample of A?(1-40). Our result suggests that A?(1-40) follows a different path for aggregation in the presence of CR.

SUBMITTER: Pratim Bose P 

PROVIDER: S-EPMC3368672 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Effects of Congo red on aβ(1-40) fibril formation process and morphology.

Pratim Bose Partha P   Chatterjee Urmimala U   Xie Ling L   Johansson Jan J   Göthelid Emmanuelle E   Arvidsson Per I PI  

ACS chemical neuroscience 20100203 4


Alzheimer's disease (AD), an age-related neurodegenerative disorder, is the most common form of dementia, and the seventh-leading cause of death in the United States. Current treatments offer only symptomatic relief; thus, there is a great need for new treatments with disease-modifying potential. One pathological hallmark of AD is so-called senile plaques, mainly made up of β-sheet-rich assemblies of 40- or 42-residue amyloid β-peptides (Aβ). Hence, inhibition of Aβ aggregation is actively explo  ...[more]

Similar Datasets

| S-EPMC6028940 | biostudies-literature
| EMPIAR-11596 | biostudies-other
| S-EPMC3414877 | biostudies-other
| S-EPMC4191606 | biostudies-literature
| S-EPMC4849547 | biostudies-literature
| S-EPMC2683116 | biostudies-literature
2010-06-19 | GSE22425 | GEO
2004-02-16 | GSE965 | GEO
2004-02-16 | GSE964 | GEO
2004-02-16 | GSE963 | GEO