Structure relationship for binding of sulfonamides and penicillins to bovine serum albumin by fluorescence probe technique

✍ Scribed by Par-Lin Hsu; Joseph K. H. Ma; H. W. Jun; Louis A. Luzzi

• Publisher: John Wiley and Sons
• Year: 1974
• Tongue: English
• Weight: 458 KB
• Volume: 63
• Category: Article
• ISSN: 0022-3549
• DOI: 10.1002/jps.2600630107

✦ Synopsis

The binding constants and the number of binding sites for the binding of 11 sulfonamide and seven penicillin derivatives to bovine serum albumin were determined using a fluorescence probe method. The results demonstrate that these drugs bind to hydrophobic sites on the serum albumin. The binding affinities of sulfonamide and penicillin are gieatly affected by their side-chain substitutions. The binding is enhanced by the hydrophobic substitutions but decreased by the hydrophilic substitutions on the parent molecules.

Keyphrases 0 Sulfonamides-relationship between structure and binding to bovine serum albumin, fluorescence probe technique, binding constants 0 Penicillins-relationship between structure and binding to bovine serum albumin, fluorescence probe technique, binding constants Binding, sulfonamides and penicillins to bovine serum albumin-effect of structure, fluorescence probe technique, binding constants 0 Fluorescence probe techniqueused to study relationship between sulfonamide and penicillin structure and their binding to bovine serum albumin

The fact that plasma protein-bound sulfonamides and penicillins are devoid of antimicrobial activity is well established (1-3). It has also been found that these drugs bind predominantly to the albumin fraction of plasma (4, 5). Although various binding 3 2 9 0, X 2 I> 1 2 3 -1 V Figure 1-Scatchard plots of 1-anilinonaphthalene-8-sulfonic acid binding to bovine serum albumin at 27" and p H 7.45. Key: 0, in the absence of drug; 0, in thepresence of 2 X M sulfaphenazole; 0, in the presence of 1 X lo-' M sulfamethoxypyridazine; A, in the presence of 5 X lo-' M sulfamethizole; and =, in the presence of 5 x lo-' M sulfadimethoxine.