Underlying the mechanism of vancomycin and human serum albumin interaction: a biophysical study.

In the present study, the binding mechanism of vancomycin with human serum albumin (HSA) was determined. Upon addition of vancomycin to HSA, the fluorescence emission was quenched and the binding constant of vancomycin with HSA was found to be 6.05 × 10(3) M(-1) at 295 K, which corresponds to -2.16 × 10(4) J·mol(-1) of free energy. The conformation of HSA was altered upon binding of vancomycin with a decrease in α helix and an increase in β sheets and random coils, suggesting partial unfolding of the secondary structure. Molecular docking experiments found that vancomycin binds strongly with HSA at the hydrophobic pocket through hydrogen bonding and van der Waals interactions. An average binding distance of 4.71 nm has been determined on the basis of the Förster resonance energy theory. It was demonstrated that vancomycin binding to HSA causes protein structural changes.