Study on the interaction of sulforaphane with human and bovine serum albumins

Sulforaphane; [1-isothiocyanato-4-(methylsulfinyl) butane], (SFN) is an isothiocyanate derived from glucoraphanin present in cruciferous vegetables and has a variety of potential chemopreventive actions. This study was designed to examine the interaction of sulforaphane with HSA and BSA. FTIR, UV–Vis spectroscopic methods as well as molecular modeling were used to determine the drug binding mode, binding constant and the effect of drug complexation on serum albumins stability and conformation. Structural analysis showed that SFN bind HSA and BSA via polypeptide polar groups with overall binding constants of KSFN–HSA = 6.54 × 104 and KSFN–BSA = 8.55 × 104 M−1. HSA and BSA conformations were altered by a major reduction of α-helix upon SFN interaction. These results suggest that serum albumins might act as carrier proteins for SFN in delivering them to target tissues.

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► SFN binds HSA via non-polar amino acids.
► SFN binds BSA via polar amino acids.
► SFN interacts with the positively charged amino acids.
► The stronger binding was observed for BSA than HSA.
► HSA and BSA might act as carrier proteins for SFN in delivering it to target molecules.