Studies on the interactions of theaflavin-3,3′-digallate with bovine serum albumin: Multi-spectroscopic analysis and molecular docking

Tea cream, produced by interactions among tea ingredients, is undesirable in tea beverage industry. The interaction between bovine serum albumin (BSA) and theaflavin-3,3'-digallate (TFDG, an important component in tea cream and functional substance of black tea) was investigated by fluorescence spectroscopy, ultraviolet-visible (UV-vis) absorption spectroscopy, synchronous fluorescence spectroscopy, fourier-transform infrared (FT-IR) spectroscopy, and molecular docking technique. Multi-spectroscopic experiments demonstrated that TFDG interacted with BSA via static quenching, and the microenvironment around BSA became more hydrophobicity. FT-IR showed that the alpha-helix of BSA was increased when binding with TFDG. Thermodynamic parameters and molecular docking demonstrated that hydrophobic interactions and hydrogen bonds dominated the interaction between TFDG and BSA. The mechanism proposed in this research could further develop some nanoparticles to excellent biochemical properties while reducing the formation of tea cream, and explore the potential of BSA as transport carrier for TFDG

Automated summary

By utilizing various experimental techniques such as fluorescence spectroscopy and UV-vis absorption spectroscopy, the interaction mechanism between theaflavin-3,3'-digallate (TFDG) and bovine serum albumin (BSA) was studied, demonstrating that hydrophobic interactions and hydrogen bonds play a dominant role in their interaction. This research provides the possibility for further development of nanoparticles with superior biochemical properties and potential exploration of BSA as a transport carrier for TFDG.