GOLD(I) WEAK BINDING SITES: HISTIDINE RESIDUES OF SERUM ALBUMIN
Weak Binding Sites of Serum Albumin and Gold(I) Compounds
publication
Author Information
Author(s): J. Xiao, C. Frank Shaw
Primary Institution: University of Wisconsin-Milwaukee
Hypothesis
Et3PAuCI binds to weak binding sites of serum albumin, specifically targeting histidine residues.
Conclusion
Et3PAu+ preferentially binds to hydrophobic histidine residues in serum albumin, causing observable changes in NMR resonances.
Supporting Evidence
- Et3PAu+ reacts with bovine serum albumin in vitro.
- 31p NMR shifts indicate the presence of weak binding sites.
- Shifting and broadening of C2H resonances were observed upon titration with Et3PAuCI.
Takeaway
This study shows that a gold compound can stick to certain parts of a protein in our blood, which might help us understand how it works in medicine.
Methodology
A 1H NMR study was performed to investigate the binding of Et3PAuCI to bovine serum albumin.
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