Aflatoxin B1 transport in rat blood plasma. Binding to albumin in vivo and in vitro and spectrofluorimetric studies into the nature of the interaction.

Binding of [3H]aflatoxin B1 to rat plasma was investigated in vivo and in vitro. Column chromatographic and polyacrylamide gel electrophoretic analyses clearly demonstrated that aflatoxin B1 bound primarily plasma albumin. Very little binding activity was shown by other plasma proteins. Spectrofluorimetric studies were undertaken to gain some insight into the nature of the aflatoxin-albumin interaction. Quenching of the lone tryptophan fluorescence intensity upon aflatoxin binding was due, at least in part, to a ligand-induced conformational change in the albumin molecule. Aflatoxin B1 binds an apolar site with an association constant of 30 mM-1 at pH 7.4 and 20 degrees C. Neither charcoal treatment of rat albumin nor the presence of 0.15 M NaCl had any significant effect on the interaction. The association constant was pH-dependent, increasing about 1.7-fold as the pH increased from 6.1 to 8.4. This pH dependence is ascribed to a pH-induced conformational change in the albumin molecule. Thermodynamic studies indicated that the aflatoxin-albumin interaction was exothermic (delta H = -29.3 kJ X mol-1), with a delta S value of -13.8 J X mol-1 X K-1.