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Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer's disease

Hayne, David J, Lim, SinChun and Donnelly, Paul S 2014, Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer's disease, Chemical society reviews, vol. 43, no. 19, pp. 6701-6715, doi: 10.1039/c4cs00026a.

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Title Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer's disease
Author(s) Hayne, David JORCID iD for Hayne, David J orcid.org/0000-0003-2756-9427
Lim, SinChun
Donnelly, Paul S
Journal name Chemical society reviews
Volume number 43
Issue number 19
Start page 6701
End page 6715
Total pages 15
Publisher Royal Society of Chemistry
Place of publication London, Eng.
Publication date 2014-10-07
ISSN 0009-2681
1460-4744
Keyword(s) Alzheimer Disease
Amyloid beta-Peptides
Animals
Brain
Coordination Complexes
Copper
Humans
Protein Binding
Radiopharmaceuticals
Technetium
Summary Alzheimer's disease is the most common form of age-related neurodegenerative dementia. The disease is characterised by the presence of plaques in the cerebral cortex. The major constituent of these plaques is aggregated amyloid-β peptide. This review focuses on the molecular aspects of metal complexes designed to bind to amyloid-β. The development of radioactive metal-based complexes of copper and technetium designed as diagnostic imaging agents to detect amyloid burden in the brain is discussed. Separate sections of the review discuss the use of luminescent metal complexes to act as non-conventional probes of amyloid formation and recent research into the use of metal complexes as inhibitors of amyloid formation and toxicity.
Language eng
DOI 10.1039/c4cs00026a
Field of Research 03 Chemical Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2014, The Authors
Free to Read? Yes
Use Rights Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30101627

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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.