Heavy metal ions are potent inhibitors of protein folding.

Details

Serval ID
serval:BIB_E427F66CB47D
Type
Article: article from journal or magazin.
Collection
Publications
Title
Heavy metal ions are potent inhibitors of protein folding.
Journal
Biochemical and Biophysical Research Communications
Author(s)
Sharma S.K., Goloubinoff P., Christen P.
ISSN
1090-2104[electronic]
Publication state
Published
Issued date
2008
Volume
372
Number
2
Pages
341-345
Language
english
Abstract
Environmental and occupational exposure to heavy metals such as cadmium, mercury and lead results in severe health hazards including prenatal and developmental defects. The deleterious effects of heavy metal ions have hitherto been attributed to their interactions with specific, particularly susceptible native proteins. Here, we report an as yet undescribed mode of heavy metal toxicity. Cd2+, Hg2+ and Pb2+ proved to inhibit very efficiently the spontaneous refolding of chemically denatured proteins by forming high-affinity multidentate complexes with thiol and other functional groups (IC(50) in the nanomolar range). With similar efficacy, the heavy metal ions inhibited the chaperone-assisted refolding of chemically denatured and heat-denatured proteins. Thus, the toxic effects of heavy metal ions may result as well from their interaction with the more readily accessible functional groups of proteins in nascent and other non-native form. The toxic scope of heavy metals seems to be substantially larger than assumed so far.
Keywords
Adenosine Triphosphatases/drug effects, Cadmium/toxicity, Cations, Divalent/pharmacology, Lead/toxicity, Luciferases/chemistry, Luciferases/drug effects, Mercury/toxicity, Metals, Heavy/toxicity, Molecular Chaperones/drug effects, Protein Folding, Protein Renaturation/drug effects
Pubmed
Web of science
Create date
30/10/2009 13:21
Last modification date
20/08/2019 17:07
Usage data