A novel vision into the binding behavior of curcumin with human serum albumin-holo transferrin complex: molecular dynamic simulation and multi-spectroscopic perspectives.

In this work, we investigated the simultaneous binding of curcumin (CUR) to human serum albumin (HSA) and human-holo transferrin (HTF) in the roles of binary and ternary systems. The binding affinity and binding site of protein-protein interaction were studied by the methods of multiple spectroscopic and molecular dynamics (MD) simulation. According to the results, the measurements for binding constant of HSA-CUR, HTF-CUR and (HSA-HTF) CUR complexes were observed to be 1.

Analysis of the interaction behavior between Nano-Curcumin and two human serum proteins: combining spectroscopy and molecular stimulation to understand protein-protein interaction.

In this study, we have investigated the effects of Nano-curcumin (Nano-CUR) binding on HSA-HTF interactions as binary and ternary systems, which had been done through multiple spectroscopic and MD simulation. It has been indicated by fluorescence spectroscopy that Nano-CUR is capable of quenching both proteins with a static mechanism. Thermodynamic parameters have been calculated by considering the fluorescence data at different temperatures.