Investigation on the interactions of silymarin to bovine serum albumin and lysozyme by fluorescence and absorbance

▶ Quenchings of BSA and LYS fluorescence by silymarin were all static quenchings. ▶ Binding constants, binding sites, and thermodynamic parameters were calculated. ▶ Hydrophobic and electrostatic forces were the major forces in the two systems. ▶ The binding of silymarin to BSA and LYS changed the conformation of BSA and LYS. ▶ Energy transfer occurred between silymarin and protein.