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The large number of synthesized azo dyes is widely applied in the food, pharmaceutical, cosmetic, textile, and leather industries. In this study, the binding mechanism of two synthesized dyes with human serum albumin (HSA); as the most abundant protein in plasma; was elucidated by fluorescence spectroscopy, Fourier-transform infrared spectroscopy and molecular modeling methods. The fluorescence quenching measurements showed that each dye can quench the intrinsic fluorescence of HSA via a dynamic quenching mechanism with an increase in concentration. From the thermodynamic data observations, revealed that the binding process is a spontaneous molecular force for each dye with HSA due to hydrophobic interactions and hydrogen bonding. FT-IR spectra showed that the secondary structure of the protein changes due to interaction of each dye with HSA. Furthermore, docking simulation demonstrated that the probable binding location of both dyes is subdomain IIA of HSA (Sudlow site I) and that complex formed is stabilized by hydrophobic interactions and hydrogen bonding. Communicated by Ramaswamy H. Sarma

Binding elucidation of azo dyes with human serum albumin via spectroscopic approaches and molecular docking techniques