The coordination chemistry of the aqua-soluble copper(I)-PTA complexes has received an increased interest in recent years. This type complexes may play an important role in the mechanism of cytotoxicity and antitumor activity. They may also be utility in positron emission tomography and targeted radiotherapy. Plasma proteins binding have profound effect on drug distribution and pharmacokinetics. Human serum albumin is the most abundant plasma protein and is responsible for the majority of known drug-protein binding interactions in blood.
In this work, our objective is to study the effect of potential copper(I) radiopharmaceutical on the albumin structure. The binding studies have been performed using spectroscopic methods – fluorescence and circular dichroism. CD spectra indicate that the metal complex-HSA interaction cause conformational changes with the loss of helical stability of protein. Fluorescence data revealed that the fluorescence quenching of HSA by copper complex was the result of the formed complex of HSA-Cu-PTA. The binding constants (Ka), number of binding sites and Stern-Volmer constants have been established.


Figure 1. Structure of the investigated copper(I) complexes and PTA ligands

Keywords: 1,3,5-triaza-7-phosphaadamantane (PTA), copper(I)-PTA complexes, human serum albumin (HSA), radiopharmaceuticals, positron emission tomography (PET)

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