Evaluation of hydrophobic interaction between acidic drugs and bovine serum albumin by reversed-phase high-performance liquid chromatography.
The contribution of hydrophobic interaction to the protein binding of acidic drugs has been evaluated in terms of a new hydrophobic index (r-value), defined as the slope of the log-log plots of capacity factor vs. reciprocal of methanol concentration in an aqueous binary mobile phase, measured by the reversed-phase high-performance liquid chromatography. The logarithms of the binding constants (log K1) of the selected acidic drugs and the related aromatic carboxylic acids indicated linear relationship with their r-values, suggesting that the effect of hydrophobicity on protein binding can be explained similarly to that on the retention onto the reversed-phase stationary ligand.
Kaibara
A
A
Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
Hirose
M
M
Nakagawa
T
T
D002264:Carboxylic Acids / Q000097:blood*; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D004364:Pharmaceutical Preparations / Q000378:metabolism*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D014867:Water
D002264:Carboxylic Acids; D004364:Pharmaceutical Preparations; D014867:Water; D012710:Serum Albumin, Bovine