Human serum transferrin (Tf) is a bilobal glycoprotein responsible for the transport and metabolism of two ferric ions. However, at only 30% saturation in human serum, reports have found that Tf can bind a variety of other metals. Titanium is naturally abundant, yet insoluble in physiological conditions, therefore, complexation with a ligand is often necessary to increase its bioavailability. The hydrolysis prone nature of Ti allows us to visualize features of its binding that have otherwise been unseen in previously utilized spectroscopic methods used to detail the Ti-Tf interaction. Titanocene dichloride (TDC) is a hydrolysis prone anticancer agent that has been shown to cause a ligand to metal charge transfer as it binds into the lobes of Tf. While TDC failed out of clinical trials, much can still be learned about the binding interactions of this model. ICP-OES was paramount in detecting those spectroscopically mute interactions. While UV/Vis proved the characteristic 2:1 metal to protein binding, ICP-OES revealed higher binding equivalents were still prevalent in solution, past that seen in controls due to hydrolysis. Further studies showed an inability of TDC to cause a typical lobe closure of Tf as would have been seen with Fe. Additionally, studies with holoTf, or Fe(III) bound Tf, still showed solubilized TDC, which speaks further on the surface binding properties of Tf and possible new pathways of Ti cellular introduction.

Superstoichiometric binding of the anticancer agent titanocene dichloride by human serum transferrin and the effects on lobe closure

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.