Investigation of the interactions of polyhedral borane anions with serum albumins

The retention of polyhedral borane anions within tumor cells has been attributed to the possible formation of covalent bonds with nucleophilic protein substituents. In an effort to identify the nature of possible interactions between polyhedral borane anions and proteins, three polyhedral borane anions, [B20H18]2−, [B20H17OH]4−, and [B20H17SH]4−, were allowed to react with either bovine or human serum albumin. Reaction products were analyzed with matrix assisted laser desorption ionization (MALDI) mass spectrometry and gel electrophoresis. Evidence of disulfide bond formation was observed with the [B20H17SH]4− anion, whereas no evidence of covalent binding was observed with the [B20H18]2− and [B20H17OH]4− ions. The potential for disulfide bond formation was confirmed by examining the reactions of the [B20H17SH]4− ion with both DTNB and reduced glutathione. An understanding of the nature of the binding will provide a basis for the design and synthesis of boron-containing compounds for application in boron neutron capture therapy.