Thermodynamic Study of Human Serum Albumin upon Interaction with Ytterbium (III)‎

Abstract EN

Complexation reaction between Yb3+ and human serum albumin is examined using isothermal titration calorimetry (ITC).

The extension solvation theory was used to reproduce the enthalpies of HAS + Yb3+ interactions over the whole range of Yb3+ concentrations.

The binding parameters recovered from this model were attributed to the structural change of HSA.

The results show that Yb3+ ions bind to HSA with three equivalent affinity sites.

It was found that in the high concentrations of the ytterbium ions, the HSA structure was destabilized.