Streptozocin; a GLUT2 binding drug, interacts with human serum albumin at loci h6-h7.

Streptozocin (STZ) is a broad range antibiotic, highly genotoxic, antineoplastic and hyperglycemic. HSA is the most abundant protein in physiology and it binds to almost all exogenic and endogenic ligands, including drugs. STZ-induced fluorescence quenching of HSA has been done at pH 7.4, pH 3.5 and at pH 7.4 with 4.5 M urea at temperatures 286 K, 291 K, and 306 K. K found to be 10 M, binding constant 1.5X10M and binding sites ~1. But, K for HSA and glucopyranose interaction was found lesser than that of HSA-STZ binding. Binding of STZ/glucopyranose on HSA seems to result in complex formation as calculated K > 10 M s. The number of binding sites, binding constants, and binding energies were increased with temperature. The ΔG, ΔH, and ΔS for HSA-STZ interaction were found to be -17.7 × 10 J·mol; 2.34 × 10 J·mol and 841 JK mol respectively at pH 7.4 and 291 K. The comparative bindings of N, F and I states of HSA with STZ and their molecular docking analyses indicate that IIIA-B junction (i.e., inter-helix h6-h7) is the probable binding site, a locus close to fatty acid binding site-5. These results could be useful for therapeutic and analytical exploitation of STZ, as albumin used as the vehicle for drug delivery.