5 research outputs found
New Supramolecular Au<sup>I</sup>–Cu<sup>I</sup> Complex as Potential Luminescent Label for Proteins
A novel
supramolecular [Au<sub>6</sub>Cu<sub>2</sub>(C<sub>2</sub>C<sub>6</sub>H<sub>4</sub>-4-COONC<sub>4</sub>H<sub>4</sub>O<sub>2</sub>)<sub>6</sub>(Ph<sub>2</sub>PC<sub>6</sub>H<sub>4</sub>PPh<sub>2</sub>)<sub>3</sub>]Â(PF<sub>6</sub>)<sub>2</sub> 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