Variation in the heats of reaction of drugs and albumin with the source and pretreatment of the albumin

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.

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Binding of tolmetin and salicylic acid to human serum albumin as a function of temperature

Behm

Flynn

Wagner

1981

Biopharm & Drug Disp

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Some novel observations of a drug (indoprofen)—albumin interaction

Juni

Nieves

Perrin

1983

Biopharm & Drug Disp

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Indoprofen, a new-steroidal anti-inflammatory agent, binds to human serum albumin in an endothermic reaction at low degrees of saturation and with an exothermic reaction at higher drug to protein ratios. Although indoprofen appears to bind to the same primary site as diazepam, dialysis studies show an increased binding of both drugs in the presence of the other. This novel observation is probably due to the effect of the drugs on the N leads to B conformational change of human serum albumin.

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Microcalorimetric investigations of drug–albumin interactions

Hardee

Fleitman

Otagiri

et al. 1984

Biopharm & Drug Disp

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Flow microcalorimetry was used to estimate primary binding constants for drug-albumin interactions. Measurements of heat of reaction at two temperatures illustrated the danger of extrapolation for pharmacokinetic purposes of measurements made at temperatures other than 37 degrees. The method could be used to predict competition between two drugs for a single binding site. Major advantages over spectroscopic techniques included direct determinations of thermodynamic parameters, and the use of physiological concentrations of albumin.

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Variation in the heats of reaction of drugs and albumin with the source and pretreatment of the albumin

Cited by 6 publications

References 3 publications

Binding of tolmetin and salicylic acid to human serum albumin as a function of temperature

Binding of tolmetin and salicylic acid to human serum albumin as a function of temperature

Some novel observations of a drug (indoprofen)—albumin interaction

Microcalorimetric investigations of drug–albumin interactions

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