The binding reaction between adriamycin (ADR) and bovine serum albumin (BSA) was investigated by absorption spectrometry and fluorescence measurement. It is proved that the fluorescence quenching of BSA by ADR is a result of the formation of ADR-BSA complex. The equilibrium constant K and the number of binding sites n were measured at different pH by fluorescence quenching method. The binding distance r and transfer efficiency E between ADR and BSA were also obtained according to Forster theory of non-radiation energy transfer. The effect of ADR on the conformation of BSA was also analyzed using synchronous fluorescence spectroscopy. By studying the binding of 7- deoxyadriamycinone to BSA, the binding mode between ADR and BSA was discussed.

Key words: adriamycin, BOVINE SERUM ALBUMIN, FLUOROSPECTROPHOTOMETRY, BINDING