Ruthenium Complexes Double-Vex Alzheimer’s Peptide | Chemical & Engineering News
Volume 91 Issue 29 | p. 27 | Concentrates
Issue Date: July 22, 2013

Ruthenium Complexes Double-Vex Alzheimer’s Peptide

Molecules light up to track amyloid-ß and may disrupt the disease-causing peptide’s aggregation pathway, hinting at a possible drug treatment
Department: Science & Technology | Collection: Life Sciences
News Channels: Biological SCENE, JACS In C&EN
Keywords: Alzheimer’s, ruthenium complex, amyloid-ß, fibrils, aggregate
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This computational model shows how a ruthenium complex binds to amyloid-β. The alignment of the complex’s bulky ligands parallel to the fibril axis (shown in red) could inhibit further amyloid-β aggregation.
Credit: J. Am. Chem. Soc.
This computational model shows how a ruthenium complex binds to amyloid-ß. The complex’s bulky ligands align parallel to the fibril axis shown in red, inhibiting further amyloid-ß aggregation.
 
This computational model shows how a ruthenium complex binds to amyloid-β. The alignment of the complex’s bulky ligands parallel to the fibril axis (shown in red) could inhibit further amyloid-β aggregation.
Credit: J. Am. Chem. Soc.

Peering inside the brain of a person with Alzheimer’s disease reveals cobwebs of disruptive fibrils made up of aggregated amyloid-β peptide. Some scientists believe the key to treating Alzheimer’s, or even preventing it, is to design molecular probes for real-time monitoring of amyloid-β and to develop drug treatments that block amyloid-β aggregation. In a new development, a team led by Angel A. Martí of Rice University and Rajeev Prabhakar of the University of Miami has uncovered that ruthenium complexes containing bulky aromatic bipyridine and dipyridophenazine ligands can perform both functions. The ruthenium complexes, which are already used in DNA detection, luminesce when they bind amyloid-β, and the researchers propose that their bulk could inhibit aggregate formation (J. Am. Chem. Soc. 2013, DOI: 10.1021/ja404850u). Using experimental and computational techniques, the researchers found that the ruthenium complexes bind to amyloid-β with the bulky ligands aligning parallel to the fibril axis. They note that the parallel binding is unprecedented for the ruthenium complexes, which align perpendicular to the axis of DNA strands. The parallel binding orientation, the researchers believe, could block amyloid aggregation. The finding opens new possibilities for using molecules with extended aromatic systems as agents to tackle Alzheimer’s, they conclude.

 
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