Multi technique investigation on interaction between 5-(2-thiazolylazo)-2,4,6-triaminopyrimidine and HSA and BSA.

In research laboratories and in various industries, azo compounds are among the most effective and commonly used organic dyes. The association between human (HSA) and bovine (BSA) serum albumins with 5-(2-thiazolylazo)-2,4,6-triaminopyrimidine (TTP) was investigated in this research using spectroscopy methods and molecular modeling study. The fluorescence quenching results showed that the quenching mechanisms were static and dynamic processes for HSA and BSA, respectively. From the thermodynamic observations, it is clear that the binding process is a spontaneous molecular interaction, in which van der Waals and hydrogen bonding interactions for HSA and hydrophobic interaction for BSA play the major roles. According to Förster energy transfer, non-radiative energy transferred from HSA and BSA to TTP, is provided by close distance ) between TTP and Trp residues of HSA and BSA. The synchronous fluorescence spectroscopy, FT-IR findings and UV-Vis absorption data confirm that TTP can induce conformational and micro environmental changes in both the proteins. Furthermore, docking results predicted the probable binding site of TTP in subdomain IIA of HSA and BSA molecules where Trp residues are located. Types of amino acid residues surrounding the TTP molecule supported that van der Waals forces, hydrophobic forces and electrostatic forces play important roles in stabilization of drug-protein complexes formed.Communicated by Ramaswamy H. Sarma.