Coordination of zinc ions to the key proteins of neurodegenerative diseases: Aβ, APP, α-synuclein and PrP
► Overview of zinc ion binding to the proteins involved in neurodegenerative diseases. ► Zinc coordnation and putative physiological relevance of the complexes. ► Zinc coordination to amyloid-β peptide may trigger the amyloid fibril formation. ► Zinc coordination to synuclein occurs only under non-p...
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Published in | Coordination chemistry reviews Vol. 256; no. 19-20; pp. 2219 - 2224 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Elsevier B.V
01.10.2012
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Subjects | |
Online Access | Get full text |
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Summary: | ► Overview of zinc ion binding to the proteins involved in neurodegenerative diseases. ► Zinc coordnation and putative physiological relevance of the complexes. ► Zinc coordination to amyloid-β peptide may trigger the amyloid fibril formation. ► Zinc coordination to synuclein occurs only under non-physiological conditions.
Major neurodegenerative disorders, including Alzheimer's and Parkinsons's disease and prion related pathologies are associated with protein misfolding and aggregation. Proteins involved in all the listed diseases are able to form complexes with metal ions and there is a dyshomeostasis and miscompartmentalization of the transition metals in the brain during these diseases. Therefore, it is important to understand the interactions between the key proteins of the neurodegenerative diseases and the transition metal ions and its consequences. We give a review on the coordination chemistry of zinc ions to Aβ, APP, α-synuclein and PrP. |
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ISSN: | 0010-8545 1873-3840 |
DOI: | 10.1016/j.ccr.2011.12.008 |