Modification of amyloid-beta peptide aggregation <i>via</i> photoactivation of strained Ru(<scp>ii</scp>) polypyridyl complexes
Janaina C. Bataglioli, Luiza Moreira Gomes, Camille Maunoir, Jason R. Smith, Houston D. Cole, Julia McCain, Tariq Sainuddin, Colin G. Cameron, Sherri A. McFarland, Tim Storr
Abstract
results in the formation of large amorphous aggregates as a common endpoint, with Ru complexes incorporating the extended phenanthroline ligand accelerating this process and thereby limiting the formation of oligomeric species in the initial stages of the aggregation process that are reported to show considerable toxicity.
Topics & Concepts
PeptideChemistryLigand (biochemistry)FibrilCovalent bondAmyloid (mycology)BiophysicsSmall moleculeStereochemistryBiochemistryReceptorBiologyOrganic chemistryInorganic chemistryAlzheimer's disease research and treatmentsSupramolecular Self-Assembly in MaterialsMolecular Sensors and Ion Detection