Radiotracer studies of the antitumor metallocene molybdocene dichloride with biomolecules

Neutron irradiation of Cp2MoCl2 for 24 h afforded the radiotracer Cp299MoCl2 which was characterised by UV–Vis spectroscopy and thin layer chromatography. Binding experiments with the thiol containing protein human serum albumin (HSA) or calf thymus DNA, were monitored for 99Mo using a gamma counter. Under the conditions investigated, molar ratios of binding of 0.2:1 (Cp2MoCl2:DNA) and 9.4:1 (Cp2MoCl2:HSA) were calculated. The results are consistent with in vitro coordination studies that have shown strong preferential interaction of Cp2MoCl2 with thiols versus other donor sites in biomolecules including DNA.

Binding experiments with the radiotracer Cp299MoCl2 and the thiol containing protein human serum albumin (HSA) or calf thymus DNA, monitored for 99Mo using a gamma counter, are consistent with strong preferential interaction of Cp2MoCl2 with thiols versus other donor sites in biomolecules including DNA.Figure optionsDownload as PowerPoint slide