Study on the Interaction Between 1,8-Ditetramethylpyrazine Based Rhein and Bovine Serum Albumin
This study employs UV spectroscopy,fluorescence spectroscopy,circular dichroism,electrochemical analysis,and molecular docking techniques to elucidate the interaction mechanism between 1,8-ditetramethylpyrazine based rhein(DBR)and bovine serum albumin(BSA).Experimental results demonstrate a strong interaction between DBR and BSA:At 290,300,and 310 K,the order of magnitude of the binding constant Ka between DBR and BSA is over 105,and the number of binding sites is 1.1,inferring a strong interaction between DBR and BSA to form a 1∶1 complex.With the Kq values are 5.5924 × 1012 L·mol-1·s-1,4.9853 × 1012 L·mol-1·s-1,4.1665 × 1012 L·mol-1·s-1,we can speculate that the quenching method is static quenching.According to Förster's non-radiative energy transfer mechanism,the binding distance r=4.8 nm and energy transfer efficiency E=0.5793 between the donor and receptor were calculated,indicating the existence of non radiative energy transfer between DBR and BSA.By calculating the thermodynamic parameters of the system,it is shown that △H＜0,△S＜0,△G＜0,indicating that the types of the two forces are hydrogen bonding and van der Waals forces.In addition,with the addition of DBR,the conformation of BSA has changed.The a-spiral structure has decreased from 60.55％to 58.5％.Electrochemical analysis shows that non-electroactive supramolecular compounds form.The molecular docking simulation results speculate that DBR molecules have entered the hydrophobic cavity of BSA molecules,and their binding sites are located in the domain Ⅰ A subdomain.
1,8-Ditetramethylpyrazine based rheinBovine serum albuminSpectroscopyElectrochemical methodMacromolecular docking
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