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

Table 1

Binding parameters for HAS + Yb³⁺ interactions. The big association equilibrium constant values show that there is strong interaction between Yb³⁺ and HSA. The entropy driven of the interaction indicates that minimizing the number of hydrophobic side chains exposed to water is the principal driving force behind the folding process. The large and negative 𝛿^𝜃𝐵 values show that HSA has been destabilized in the high concentrations of Yb³⁺ ions.

Parameters	T = 300 K	T = 310 K
𝐾𝑎/L·mol^−1	5.59×10^5±210	9.17×10^5±210
p	1±0.01	1±0.01
𝛿^𝜃𝐴	29.04±0.14	14.05±0.14
𝛿^𝜃𝐵	−53.22±0.16	−71.57±0.16
ΔH/kJ mol^−1	30.78±0.09	45.7±0.09
ΔG/kJ mol^−1	−33±0.07	−34.24±0.07
ΔS/kJ mol^−1 K^−1	0.21±0.02	0.25±0.02