The binding of benzopyranes to human serum albumin. A structure-affinity study.
The binding of several benzopyranes to serum albumin was studied by equilibrium dialysis at pH 7.4 in a 67 mM sodium phosphate buffer at 37 degrees C. The equilibrium data were analyzed using a computer program for curve fitting. The binding isotherm for warfarin, 4-hydroxycoumarin, 4-chromanol, coumarin, 3-acetylcoumarin, and benzoic acid can be described by two stoichiometric dissociation constants. Elimination of the 4-hydroxyl group in the coumarin chemical structures decreases the binding affinity of the compounds on the primary binding site of serum albumin, with 4-chromanol the smallest ligand which binds to seroalbumin with high affinity. Thus, the affinity of 4-benzopyranol and the 4-hydroxybenzopyranones greater than that of benzopyranones. On the other hand, elimination of the 2-oxo group in the benzopyranone chemical structures decreases affinity for the secondary binding site.
Ferrer
J M
JM
Departamento de Bioquímica y Biología Molecular, Facultad de Farmacia, Universidad del País Vasco, Vitoria, Spain.
Leiton
M J
MJ
Zatón
A M
AM
D001665:Binding Sites; D002839:Chromans / Q000378:metabolism*; D003374:Coumarins / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014859:Warfarin / Q000378:metabolism*
D002839:Chromans; D003374:Coumarins; D012709:Serum Albumin; D014859:Warfarin; C029141:2,2,5,7,8-pentamethyl-1-hydroxychroman