Abstract: AimTo study the interaction between strychnine and bovine serum albumin. Methods Fluorescence spectroscopy and ultraviolet spectroscopy were used. ResultsThe static quenching and the non-radiation energy transfer are the two main reasons to leading the fluorescence quenching of BSA. The apparent combining constants (k_a) between strychnine and BSA are 3.72×10³ at 27 ℃, 4.27×10³ at 37 ℃, 4.47×10³ at 47 ℃ and the combining sites are 1.01±0.03. The combining distance (r=3.795 nm) and energy transfer efficiency (e=0.033 8) are obtained by Frster’s non-radiation energy transfer mechanism. ConclusionThe interaction between strychnine and BSA was driven mainly by hydrophobic force.