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Amyloid-β and α-synuclein decrease the level of metal-catalyzed reactive oxygen species by radical scavenging and redox silencing

Publication: Research - peer-reviewJournal article

Documents

Jeppe Trudslev Pedersen, Serene W. Chen, Christian Bernsen Borg, Samuel Ness, Justyna M. Bahl, Niels H. H. Heegard, Christopher M. Dobson, Lars Bo Stegeager Hemmingsen, Nunilo Cremades, Kaare Teilum

The formation of reactive oxygen species (ROS) is linked to the pathogenesis of Alzheimer's and Parkinson's diseases. Here we have investigated the effect of soluble and aggregated Aβ and α-synuclein, associated with Alzheimer's and Parkinson's disease respectively, on the Cu2+-catalyzed formation of ROS in vitro in the presence of a biological reductant. We find that the levels of ROS, and the rate by which ROS is generated, are significantly reduced when the Cu2+ is bound to Aβ or α-synuclein, particularly when they are in the oligomeric or fibrillar forms. This effect is attributed to a combination of radical scavenging and redox silencing mechanisms. Our findings suggest that the increase in ROS associated with the accumulation of aggregated Aβ or α-synuclein does not result from a particularly ROS-active form of these peptides, but rather from either a local increase of Cu2+ and other ROS-active metal ions in the aggregates or as a downstream consequence of the formation of the patho-logical amyloid structures.

Original languageEnglish
JournalJournal of the American Chemical Society
Volume138
Issue number12
Pages (from-to)3966-3969
Number of pages4
ISSN0002-7863
DOIs
StatePublished - 2016

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