Journal article
Rhenium and technetium complexes that bind to amyloid-β plaques
DJ Hayne, AJ North, M Fodero-Tavoletti, JM White, LW Hung, A Rigopoulos, CA Mclean, PA Adlard, U Ackermann, H Tochon-Danguy, VL Villemagne, KJ Barnham, PS Donnelly
Dalton Transactions | Published : 2015
DOI: 10.1039/c4dt02969k
Abstract
Alzheimer's disease is associated with the presence of insoluble protein deposits in the brain called amyloid plaques. The major constituent of these deposits is aggregated amyloid-β peptide. Technetium-99m complexes that bind to amyloid-β plaques could provide important diagnostic information on amyloid-β plaque burden using Single Photon Emission Computed Tomography (SPECT). Tridentate ligands with a stilbene functional group were used to form complexes with the fac-[MI(CO)3]+ (M = Re or 99mTc) core. The rhenium carbonyl complexes with tridentate co-ligands that included a stilbene functional group and a dimethylamino substituent bound to amyloid-β present in human frontal cortex brain tis..
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Funding Acknowledgements
The Australian Research Council is acknowledged for financial support. Covidien Ltd. provided the 'Isolink' kits used in this research. Dr Nouria Salehi (Royal Melbourne Hospital, Melbourne, Australia) is acknowledged for assistance in analysing biodistribution data. The Victorian Brain Bank is acknowledged for the provision of the brain tissue used in this study.