Role of electrostatic forces in hydroxy and keto bile salt-albumin interactions: some experimental observations.
Proton binding to bovine serum albumin and effects on hydroxy and keto bile salts-albumin binding were studied within a pH range between 5 and 10. Electrostatic forces contribute to the binding of these ligands to albumin; prototropic groups of albumin such as imidazol are involved in the interaction. Bile salts binding produces a shift in pK of these groups. It is postulated that hydroxy bile salt-albumin binding is linked with the N in equilibrium with B transition of the protein, while for keto bile salts a microarrangement in the protein binding sites is driving the interaction.
Farruggia
B
B
Departamento de Quimica-Fisica, Facultad de Ciencias Bioquimicas y Farmaceuticas, Universidad Nacional de Rosario, Argentina.
Picó
G
G
D001647:Bile Acids and Salts / Q000378:metabolism*; D004563:Electrochemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013329:Structure-Activity Relationship
D001647:Bile Acids and Salts; D012710:Serum Albumin, Bovine