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Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
Published on: May 13, 2010
Sensing and inhibition of amyloid-β based on the simple luminescent aptamer-ruthenium complex system
Eththilu Babu1, Paulpandian Muthu Mareeswaran2, Veerasamy Sathish3
1Department of Physical Chemistry, School of Chemistry, Madurai Kamaraj University, Madurai, Tamil Nadu, India; Department of Chemistry, VV College of Engineering, Tisaiyanvilai, Tamil Nadu, India.
Abstract:
Aggregation of amyloid-β (Aβ) peptide has been known to be pathologically associated with Alzheimer and dementia diseases. Amyloid-β fibrils serve as an important target for the drugs development and diagnosis of neurodegenerative diseases. Herein, we report a new [Ru(dmbpy)(dcbpy)dppz)] complex (dmbpy; 4,4'-dimethyl-2,2'-bipyridine, dcbpy; 4,4'-dicorboxy-2,2'-bipyridine, dppz; dipyridophenazine) intercalated aptamer based recognition of amyloid-β. Interestingly, aforementioned Ru(II) complex shows weak luminescence intensity in the aqueous medium but it shows strong luminescence intensity in the presence of RNA aptamer. Upon addition of amyloid-β monomers, the luminescence intensity of Ru(II) complex is reduced due to the strong interaction of aptamer with amyloid-β monomer/small oligomers. Furthermore, present study implies that our system has ability to inhibit the formation of amyloid-β fibrils, which is confirmed from the AFM morphological structures in the absence and presence of aptamer. This work may contribute the rapid diagnosis and inhibition of amyloid-β aggregation in the clinical applications.
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