Relationship between lipophilicity and binding to human serum albumin of arylpropionic acid non-steroidal anti-inflammatory drugs.
A possible relationship between lipophilicity and binding to human serum albumin was investigated for 11 arylpropionate non-steroidal anti-inflammatory drugs. The lipophilic parameter was determined by a reversed-phase high-performance liquid chromatographic procedure as the capacity factor (k'). The binding of arylpropionic acids to human serum albumin was studied in vitro by equilibrium dialysis. For each compound, a Scatchard analysis was performed considering two classes of binding sites characterized by high- and low-affinity constants, K1 and K2, respectively. A linear relationship was found between lipophilicity and binding parameters, n1K1 (r = 0.88, P < 0.0005) and n2K2 (r = 0.96, P < 0.0002). These results suggest the role of hydrophobic interactions in the binding of arylpropionic acids to human serum albumin.
Deschamps-Labat
L
L
Department of Pharmacology, Groupe hospitalier Pellegrin, Université de Bordeaux II, France.
Péhourcq
F
F
Jagou
M
M
Bannwarth
B
B
D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D003956:Dialysis; D006801:Humans; D008956:Models, Chemical; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
D000894:Anti-Inflammatory Agents, Non-Steroidal; D012709:Serum Albumin