Gold-Induced Structural Switch of Cys34 in Albumin: Comparison of Auranofin with Aurothiomalate
Gold-Induced Changes in Albumin Structure
publication
Author Information
Author(s): John Christodoulou, Peter J. Sadler, Slan Tucker
Primary Institution: Department of Chemistry, Birkbeck College, University of London
Hypothesis
The study investigates how gold drugs affect the structure of albumin by binding to Cys34.
Conclusion
Gold binding to albumin induces structural changes that may affect its metabolism and binding properties.
Supporting Evidence
- The primary binding site for gold on albumin is at the sulfur of Cys34.
- Structural changes in albumin were observed when treated with auranofin and aurothiomalate.
- Gold binding can switch the conformation of Cys34 from buried to exposed.
Takeaway
When gold drugs attach to a protein called albumin, they can change its shape, which might affect how the body uses the drug.
Methodology
The study used NMR spectroscopy to investigate structural changes in bovine and human albumin.
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