Multispectral and computational probing of the interactions between sitagliptin and serum albumin.

The binding of sitagliptin (SIT), an anti-diabetic drug, to human and bovine serum albumin (HSA and BSA; main serum transport proteins) was investigated using various spectroscopic and molecular docking techniques. The fluorescence data demonstrated that SIT quenched inherent fluorescence of these proteins through the formation of SIT-HSA/BSA complexes. The number of binding sites was obtained (~1) and binding constant (K) and effective quenching constant (K) were calculated as 10 for both systems.