11B nuclear magnetic resonance studies of the interaction of borocaptate sodium with serum albumin.

The interaction between borocaptate sodium, Na2B12H11SH (BSH), and three types of serum albumin--bovine, human and dog (BSA, HSA and DSA)--has been investigated quantitatively using 11B NMR. The 11B chemical shifts and relaxation rates of BSH were studied with various concentrations of serum albumin (1-5%, w/v) at 295-310 degrees K. Correction of the longitudinal relaxation rate (R1) due to protein viscosity effects was accomplished. The corrected R1 values were analyzed mathematically using a saturation function and linear regression. The linewidths of 11B resonances, which are related to the spin-spin relaxation rates (R2), were also measured. The binding fractions (P), the number of binding sites (NBS), and the binding constants (Kb) of BSH at various concentrations of the three types of serum albumin (1-5%, w/v) were determined at 295 and 310 degrees K. We speculate that the nature of this interaction may be electrostatic.