Correlation of hydrophobicity with protein binding for clorobiocin analogs.
A new method of equilibrium dialysis was used to measure the binding of analogs of clorobiocin (18631 R.P.) to human serum albumin. Binding constants and numbers of binding sites on human serum albumin were calculated from the binding data and were used to calculate the percentage of compounds free in equilibrium with 4% albumin. Partition coefficients between n-octanol and phosphate buffer (0.05 M, pH 7.4) also were measured. A positive linear correlation (r = 0.918, s = 0.240, and n = 10) was obtained between log (bound/free compound) and log partition coefficient.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003956:Dialysis; D006801:Humans; D009675:Novobiocin / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism; D012995:Solubility; D013056:Spectrophotometry, Ultraviolet
D012709:Serum Albumin; D009675:Novobiocin; C006260:clorobiocin