title: Drug-protein interaction: plasma protein binding of furocoumarins.
abstract: The binding of six furocoumarins (angelicin, psoralen, 8-methoxypsoralen, 5-methoxypsoralen, 8-methylpsoralen, 4,5'8-trimethylpsoralen) to human serum and human serum albumin was studied by equilibrium dialysis using tritium labelled compounds. The results indicated that in serum all furocoumarins are bound mostly by albumin, the extent of binding being related to the structure of the furocoumarins; at any rate, high values of the bound drug, ranging from 84 to 97% were observed. The percentage of binding is strictly related to the water solubility of the compounds. A limited number of binding sites, n = 1-2.4, were detected in the albumin molecule, indicating a high specificity in the binding process. The association constants of the furocoumarins to albumin. Ka, ranged from 1.2 X 10(4) M-1 (8-methoxypsoralen) to 1.9 X 10(5) M-1 (4,5'8-trimethylpsoralen).
mesh_terms: D001682:Biological Availability; D001798:Blood Proteins / Q000378:metabolism*; D011564:Furocoumarins / Q000097:blood / Q000494:pharmacology*; D006801:Humans; D011485:Protein Binding / Q000187:drug effects; D012709:Serum Albumin / Q000378:metabolism; D012995:Solubility
chemical_list: D001798:Blood Proteins; D011564:Furocoumarins; D012709:Serum Albumin