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Issue 13, 2004
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Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases

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Abstract

A change of the prion protein conformation results in a class of neurodegenerative diseases called the transmissible spongiform encephalopathies (like mad cow and Creutzfeld–Jakob diseases). The function of the normal prion protein is unknown, although much of recent research demonstrates the it may be a copper binding protein selective for Cu(II). Amyloid precursor protein (APP) releases the 39–42 amino acid peptide, a major constituent of the deposit in plaques of Alzheimer disease brain. Also APP is a metal binding protein, including copper ions. The link between copper and both proteins may provide insight into the role of metals in neurodegenerative pathologies.

Graphical abstract: Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases

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Publication details

The article was received on 09 Feb 2004, accepted on 21 Apr 2004 and first published on 11 May 2004


Article type: Perspective
DOI: 10.1039/B401985G
Citation: Dalton Trans., 2004, 1907-1917
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    Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases

    D. R. Brown and H. Kozlowski, Dalton Trans., 2004, 1907
    DOI: 10.1039/B401985G

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