Estimation of buspirone-bovine serum albumin binding by affinity capillary electrophoresis.
Drug-protein binding is an important process in pharmacokinetic phase of drug action. Capillary electrophoresis was employed, specifically the Hummel-Dreyer method and Scatchard analysis, to study the interactions of an anxiolytic drug, buspirone, with pure bovine serum albumin (BSA) and with BSA present in the human recombinant 5-HT(1A) serotonin receptor preparation. The binding constant of buspirone with BSA determined in free BSA solution was K = 5.55 x 10(4) M(-1) whereas its value with BSA present in the serotonin receptor preparation was K = 5.57 x 10(4) M(-1). The method was found to be inadequate for measuring the specific binding interactions between buspirone and the 5-HT(1A) receptor in the preparation employed.
Markuszewski
M
M
Department of Biopharmaceutics and Pharmacodynamics, Medical University of Gdańsk, Poland.
Frackowiak
T
T
Kaliszan
R
R
D000818:Animals; D002065:Buspirone / Q000737:chemistry / Q000378:metabolism*; D002460:Cell Line; D019075:Electrophoresis, Capillary; D006801:Humans; D011485:Protein Binding; D011985:Receptors, Serotonin / Q000378:metabolism; D044263:Receptors, Serotonin, 5-HT1; D011994:Recombinant Proteins / Q000378:metabolism; D017366:Serotonin Receptor Agonists / Q000737:chemistry / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*
D011985:Receptors, Serotonin; D044263:Receptors, Serotonin, 5-HT1; D011994:Recombinant Proteins; D017366:Serotonin Receptor Agonists; D012710:Serum Albumin, Bovine; D002065:Buspirone