- Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences
Bose, Partha Pratim; Chatterjee, Urmimala; Xie, Ling; Johansson, Jan; Gothelid, Emmanuelle; Arvidsson, Per I.
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 beta-sheet-rich assemblies of 40- or 42-residue amyloid beta-peptides (A beta). Hence, inhibition of A beta 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 beta 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 beta(1-40). Our result suggests that A beta(1-40) follows a different path for aggregation in the presence of CR.
Alzheimer's disease; atomic force microscopy; Congo red; amyloid; oligomers; fibrils; aggregates; amyloid beta-peptide
ACS Chemical Neuroscience
2010, Volume: 1, number: 4, pages: 315-324
Publisher: AMER CHEMICAL SOC
Biochemistry and Molecular Biology