Effective binding of perhalogenated closo-borates to serum albumins revealed by spectroscopic and ITC studies.

The interactions of boron cluster compounds c loso -borates with biomolecules are widely studied due to their efficiency as agents for boron neutron capture therapy of cancer. In present work the binding abilities of anionic halogen closo -borates [B 10 Hal 10 ] 2− (Hal = Cl, Br, I) and [B 12 Hal 12 ] 2− (Hal = Cl, I) towards bovine and human serum albumins were investigated by spectroscopic and isothermal titration calorimetry (ITC) methods. The protein fluorescence quenching method and ITC studies confirmed the complex formation. The degree of protein fluorescence quenching increased from chlorine to iodine boron derivatives that is attributed to external heavy atom effect. The ITC data point on the existence in the protein structure of two types of binding sites: with higher and lower affinity to closo -borates. Albumin- closo -borate complex binding ratio, n (4–5 anions per protein molecule) is higher than for the parent hydrogen closo- borates (2 anions per protein molecule). Binding constants estimated by fluorescent and ITC methods indicate higher affinity of halogen closo -borates to albumins (K in the range of 10 4 –10 6 M −1 ) comparing to that of the hydrogen closo- borate (K about 10 3 M −1 ). Due to their high affinity and high binding ratio to albumins halogen closo- borates are proposed for further studies as agents for boron neutron capture therapy. [ABSTRACT FROM AUTHOR]