Thermodynamic parameters for binding of fatty acids to human serum albumin.
Binding of laurate and myristate anions to human serum albumin has been studied over a range of temperatures, 5-37 degrees C, at pH 7.4. The binding curves indicate that the strength of binding of the first few molecules of fatty acid to albumin (r less than 5) decreases with increasing temperature, whereas binding of the following molecules seems to proceed independently of temperature. Binding data were analyzed according to the general binding equation yielding several sets of acceptable binding constants within a probability limit of 0.75. From the temperature dependence of the first step constant, it was possible to calculate values for the changes in enthalpy and entropy during the initial binding step. For the medium-chain fatty acids, laurate and myristate, binding of the first molecule to albumin appeared to be enthalpic, with a tendency to an increasing contribution of entropy to binding energy with increasing chain length of the fatty acid.
Pedersen
A O
AO
Institute of Medical Biochemistry, Aarhus University, Denmark.
Honoré
B
B
Brodersen
R
R
D006801:Humans; D007700:Kinetics; D007850:Lauric Acids / Q000378:metabolism*; D008433:Mathematics; D008962:Models, Theoretical; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013816:Thermodynamics
D007850:Lauric Acids; D009227:Myristic Acids; D012709:Serum Albumin; D019814:Myristic Acid; C030358:lauric acid