The interactions of bovine serum albumin (BSA) with five novel silicon (Ⅳ) phthalocyanines(SiPc1-5) axially modified by nucleosides (cytidine, 5-N-cytidine, methyl cytidine, uridine and methyl uridine) derivatives were studied by fluorescence spectroscopy. The results show that there are strong interactions between these silicon phthalocyanines and BSA with a binding constant of(4.90~83.18)×105 mol-1·L. Therefore, the non-covalent BSA conjugate of bis(2’,3’-O-isopropyl-cytidine-oxy) phthalocyaninatosilicon(Ⅳ) (SiPc1) was further been prepared. The molar ratio of phthalocyanine to albumin was found to be 1∶1 for the obtained SiPc1-BSA conjugate. The absorption spectra of SiPc1 and SiPc1-BSA in the visible region have no significant difference, both showing an Q-band maximum at about 686 nm. It indicates that the spectroscopic characteristics of SiPc1 are not affected by binding to albumin. The SiPc1-BSA conjugate exhibits high photodynamic activity against human hepatoma cell line HepG2 with an IC50 value of 3.0×10-7 mol·L-1. By comparsion, SiPc1-BSA has a higher photodynamic activity than SiPc1 (in PBS formation, IC50=7.0×10-7 mol·L-1), which can be attributed to its higher cellular uptake.