X-RAY CRYSTAL STRUCTURE AND SOLUTION PROPERTIES OF [Au(III)(H.2-Gly-Gly-L-His)]CI.H20
Study of Gold(III) Peptide Complexes
publication
Author Information
Author(s): Sabine L. Best, Tapan K. Chattopadhyay, Milos I. Djuran, Muhammed A. Mazid, Rex A. Palmer, Peter Sadler
Primary Institution: Birkbeck College, University of London
Hypothesis
The binding of Au(III) to peptides may be involved in delayed hypersensitivity reactions in patients undergoing chrysotherapy.
Conclusion
The crystal structure of the Au(III) peptide complex was determined, revealing a square-planar configuration.
Supporting Evidence
- Gold(III) generated via myeloperoxidase is thought to play an important role in the side-effects of anti-arthritic gold drugs.
- Only one crystal structure of a Au(III) peptide has previously been described.
- The reaction of GGH with NaAuCl4 at low pH is slow and involves one intermediate.
Takeaway
The researchers looked at how a gold compound interacts with a specific peptide, which could help explain some side effects of gold drugs.
Methodology
X-ray crystallography was used to determine the structure of the Au(III) peptide complex.
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