Purpure-18-imide was synthesized based on the porphyrin's special affinity for cancer cells and the antitumor activity of pyrrolidine compound. The binding reaction between purpure-18-imide and bovine serum albumins (BSA) in aqueous was studied by fluorescence and UV-Vis absorption spectra. The research results indicated that the combination reaction of them was a single static quenching process. In aqueous, purpure-18-imide strongly bound BSA with molar ratio of 1:1. The binding constant K0 was 5.386 x 10(5) L x mol(-1). The shortest binding distance (r = 3.54 nm) and energy transfer efficiencies (E = 0.26) between donor (BSA) and acceptor (purpure-18-imide) were obtained by Forster's nonradiative energy transfer mechanism.