Study of the binding of antibiotics to human serum albumin by charge-transfer chromatography.
The interaction of 13 antibiotics with human serum albumin was studied by charge-transfer reversed-phase thin-layer chromatography in neutral, acidic, basic and ionic environments (NaCl and MgCl2) and the relative strength of interaction was calculated. The pH and the presence of mono- and divalent cations markedly influenced the strength of interaction. The capacity of antibiotics to interact with HSA also considerably depended on their chemical structure.
Cserháti
T
T
Central Research Institute for Chemistry, Hungarian Academy of Sciences, Budapest, Hungary.
Forgács
E
E
D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002855:Chromatography, Thin Layer; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet
D000900:Anti-Bacterial Agents; D012709:Serum Albumin