Effect of pH and small inorganic ions on binding of sulfadimethoxine and sulfaphenazole to human serum albumin measured by circular dichroism.
The binding of sulfadimethoxine and sulfaphenazole to human serum albumin (HSA) has been shown by circular dichroism measurements to be dependent on the N-B transition. The secondary drug binding sites were found to be optically active in the B conformation form in HSA but optically inactive in the N form. Moreover, the drug-HSA interaction in Tris-HCl buffer seems to be more sensitive to the conformational change in HSA, compared with that in the phosphate buffer.
Otagiri
M
M
Nakamura
H
H
Imamura
Y
Y
Matsumoto
U
U
Fleitman
J
J
Perrin
J H
JH
D002942:Circular Dichroism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013412:Sulfadimethoxine / Q000097:blood*; D013426:Sulfaphenazole / Q000097:blood*
D012709:Serum Albumin; D013426:Sulfaphenazole; D013412:Sulfadimethoxine