Interaction between strychnine and bovine serum albumin

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.