BINDING OF ANTICANCER DRUGS TO HUMAN SERUM-ALBUMIN STUDIED BY REVERSED-PHASE CHROMATOGRAPHY

The interaction of eight commercial anticancer drugs with human serum albumin (HSA) was studied by charge-transfer reversed-phase thin-layer chromatography in neutral, acidic, basic and ionic environments (NaCl and CaCl2) and the relative strength of interaction was calculated. Each drug interacted with HSA in a neutral environment, and the pH and the presence of mono- and divalent cations markedly affected the strength of interaction. The capacity of anticancer drugs to interact with HSA depended considerably on their molecular structure. Various multivariate statistical methods such as principal component analysis and cluster analysis indicated that the steric parameters of anticancer drugs have a considerable impact on their capacity to bind to HSA. The influence of electronic parameters on the HSA-drug interaction was of secondary importance.