Binding of tolmetin and salicylic acid to human serum albumin as a function of temperature.
When drug-protein binding data are evaluated thermodynamically standard free energy (delta G0), standard enthalpy (delta H0) and standard entropy (delta S0) are usually estimated from association constants (Ka) derived from binding data obtained at only two temperatures. Estimation of delta H0 involves the assumption of its constancy in the temperature range studied and linearity of a van't Hoff plot of ln Ka versus 1/T. Sometimes the assumption of such linearity is invalid for theoretical reasons and data obtained at only two temperatures contain no information concerning linearity of this plot. We present data for the binding of both tolmetin and salicylic acid to human serum albumin as a function of temperature which make doubtful the validity of using association constants of these drugs to derive thermodynamic constants other than delta G0 values.
D001665:Binding Sites; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D011485:Protein Binding; D011758:Pyrroles / Q000097:blood*; D012459:Salicylates / Q000097:blood*; D020156:Salicylic Acid; D012709:Serum Albumin / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics; D014046:Tolmetin / Q000097:blood*
D011758:Pyrroles; D012459:Salicylates; D012709:Serum Albumin; D014046:Tolmetin; D020156:Salicylic Acid