Protein-drug conjugates are a rapidly expanding family of therapeutics that hold significant potential to ameliorate off-target toxic effects commonly observed in patients undergoing chemotherapy. In this context, the protein acts as a nanoscale delivery vector that alters the biodistribution of the drug upon administration by restricting its unhindered distribution in vivo. Researchers at TWU are exploring the use of cobalt coordination chemistry in the synthesis of doxorubicin-albumin conjugates. Previous work has shown that cobalt can be used to crosslink amine-containing molecules in a reversible reaction that only utilizes the lone pair of electrons on nitrogen to form a dative bond with cobalt. Doxorubicin was chosen for initial studies because it contains a primary amine that could be crosslinked with lysine residues on a protein to form a protein-drug conjugate. Initial studies showed that the number of dox molecules bound per protein could be systematically varied in the range of 1-10. However, during synthesis the solution pH was raised to 10, which could impact the protein’s tertiary structure and potentially result in denaturation. The purpose of the current study was to evaluate the thermal denaturation and stability of doxorubicin-albumin conjugates by differential scanning calorimetry to further investigate this aspect. Results of DSC experiments will be discussed.

Synthesis of doxorubicin-albumin conjugates via cobalt coordination chemistry: Effect of reaction conditions on overall protein stability

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.