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Updated: May 6, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
New supramolecular Au(I)-Cu(I) complex as potential luminescent label for proteins
D V Krupenya1, P A Snegurov, E V Grachova
1Department of Chemistry, St. Petersburg State University , Universitesky pr. 26, 198504 St. Petersburg, Russia.
Abstract:
A novel supramolecular [Au6Cu2(C2C6H4-4-COONC4H4O2)6(Ph2PC6H4PPh2)3](PF6)2 complex functionalized with a succinimide ester alkynyl substituent has been synthesized and characterized using X-ray crystallography, mass spectrometry, and NMR spectroscopy. Like the other complexes of this class, it demonstrates bright emission in acetone and dichloromethane solutions with the excited state lifetime in a microsecond domain. This complex readily reacts with a surface amine group of proteins/enzymes (human serum albumin (HSA), rabbit anti-HSA antibodies, soybean trypsin inhibitor, and α-chymotrypsin) to give covalent conjugates, which contain up to five molecules of the luminescent label bound to the biomolecule. The conjugates keep a high level of the phosphorescent label emission, but in contrast to the parent complex molecule, display excellent solubility and high stability in physiological media. Investigation of the biological activity of the conjugates also showed that the specific structure of the biomolecules remained nearly unchanged upon bonding with the label, which is indicative of a very prospective of the conjugates application in biomolecular detection.
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