Multi Technique Investigation on Binding Interaction between 5-(2-Thiazolylazo)-2,4,6-Triaminopyrimidine and Hsa and Bsa

Abstract

In research laboratories and various industries, azo compounds are among the most effective and commonly used organic dyes. Throughout this research the interaction between human and bovine serum albumins with 5-(2-Thiazolylazo)-2,4,6-Triaminopyrimidine (TTP) was explored using methods of spectroscopy and analysis of molecular modeling. The fluorescence quenching results revealed that static and dynamic processes are the quenching mechanisms for human and bovine serum albumins, respectively. The results of the quenching experiment were used to measure thermodynamic parameters [[EQUATION]] which showed that the binding process that takes place spontaneously and revealed that human and bovine serum albumins are very firmly binding through hydrogen bonds, van der Waals forces interactions and electrostatic forces. Calculations of Fӧrster energy transfer, synchronous fluorescence spectroscopy and docking analysis showed TTP bindings in short distances to the Trp residues of human and bovine serum albumin molecules. Docking study showed that TTP molecule has four hydrogen bonds with HSA, two hydrogen bonds with BSA and several hydrophobic contacts with human and bovine serum albumins. FT-IR results showed that serum albumins interact with TTP molecule primarily through hydrophobic and hydrophilic interactions, and that the secondary structure of serum albumins is modified.