Abstract
Theaflavins (TFs), bioactive compounds present in black tea manufactured from Camellia sinensis leaves have potential health benefits. Due to their instability and low bioavailability, we have encapsulated TFs into albumin nanoparticles (Alb-TFs-NP) and characterized them using different techniques. The mean particle size of Alb-TFs-NP was 125.9 nm with a low (0.23) polydispersity index and Zeta potential of -76.8 mV. Scanning electron microscopy (SEM) and Transmission electron microscopy (TEM) analysis revealed a spherical shape of Alb-TFs-NP with a smooth surface. The fluorescence of bovine serum albumin (BSA) and TFs was at 280 nm and 660 nm excitation and 690-700 nm emission respectively. The BSA-TFs complex interacts at distinct amino acid binding sites with good docking energy of TF1 (-10.5 kcal/mol-1), TF2 (-11.1 kcal/mol-1), TF2a (-11.2 kcal/mol-1) and TF3 (-10.4 kcal/mol-1) at the BSA active site. Primarily hydrogen bonding was involved in the BSA-TFs interaction. The study could further research the transport distribution and bioactivities of TFs in the human body.
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