Karp W B, Subramanyam S B, Robertson A F
J Pharm Sci. 1985 Jun;74(6):690-1. doi: 10.1002/jps.2600740624.
The binding of dapsone, 4,4'-sulfonylbis(aniline)(1), and its diacetylated derivative, 4,4"'-sulfonylbis(acetanilide)(2), to human serum albumin is reported. To assess the ability of these compounds to displace 4'-[(4-aminophenyl)sulfonyl]acetanilide (3) from albumin, a dialysis rate technique was used. Competition for the bilirubin binding site on albumin was measured with the peroxidase assay. Compounds 1 and 2 strongly displaced both 3 and bilirubin from human serum albumin. The association constants for 1 and 2 with respect to bilirubin binding were 1.29 X 10(3) and 1.15 X 10(4) M-1, respectively. These results suggest that the binding site for 3 and the bilirubin binding site are similar with respect to 1 and 2 and that the binding of dapsone and its derivatives probably does not involve the amino function.
本文报道了氨苯砜、4,4'-磺酰基双(苯胺)(1)及其二乙酰化衍生物4,4''-磺酰基双(乙酰苯胺)(2)与人血清白蛋白的结合情况。为评估这些化合物从白蛋白上取代4'-[(4-氨基苯基)磺酰基]乙酰苯胺(3)的能力，采用了透析速率技术。用过氧化物酶法测定了它们对白蛋白上胆红素结合位点的竞争情况。化合物1和2能从人血清白蛋白上强烈取代3和胆红素。1和2与胆红素结合的缔合常数分别为1.29×10³和1.15×10⁴M⁻¹。这些结果表明，就1和2而言，3的结合位点与胆红素结合位点相似，并且氨苯砜及其衍生物的结合可能不涉及氨基官能团。
