Abstract
The mechanism of the binding of several sulfonamides to bovine serum albumin has been investigated by relaxation time measurements on their high resolution proton magnetic resonance spectra. Upon addition of albumin to the sulfonamide solutions generally a larger increment in the relaxation rate was found for the p-aminobenzenesulfonamide moiety than for any of the substituents on N-1, indicating that the parent molecule is the primary binding site. The three-ring compound sulfaphenazole was found to be an exception. Two of the three rings, the p-aminobenzene sulfonamide and the phenyl portion of the N-1 substituent, bind independently. The two binding sites can be clearly distinguished since phenylpropanol interferes with the binding of the p-aminobenzenesulfonamide moiety and slightly enhances the binding of the phenyl group.
ACKNOWLEDGMENTS The authors are very much indebted to Miss Virginia L. Seery for an extensive survey of line widths on a large series of sulfonamide derivatives, and for viscosity measurements, and to Mr. Clayton Cowing for excellent maintenance and operation of the spectrometer. This work has been supported by National Science Foundation Grant GB-2612 and by U.S. Public Health Service Grants GM-09591 and 2-K3-GM-15,379.
- Copyright ©, 1965, by Academic Press Inc.
MolPharm articles become freely available 12 months after publication, and remain freely available for 5 years.Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page.
|
