In the present study the interaction of the chemotherapeutic agent, Azure A (AZA) with Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) was investigated by multi spectroscopic and molecular docking methods.
In the present investigation, we have systematically studied the binding mechanism of model protein human serum albumin (HSA) with gold/silver alloy nanoparticles (Au/Ag NPs) using multiple spectroscopic techniques. Absorption spectral studies of Au/Ag NPs in the presence of increasing concentrations of HSA resulted in a slight red shift of the surface plasmon resonance band (SPR) of Au/Ag NPs, suggesting changes in the refractive index around the nanoparticle surface owing to the adsorption of HSA. The results from high-resolution transmission electron microscopy (HR-TEM), dynamic light scattering (DLS), and zeta potential analysis substantiated the formation of a dense layer of HSA on the surface of Au/Ag NPs. The formation of a ground-state complex between HSA and Au/Ag NPs was evident from the outcome of the steady-state emission titration experiments of the HSA-Au/Ag NPs system. The binding parameters computed from corrected emission quenching data revealed that HSA exhibited a significant binding affinity toward Au/Ag NPs. The identical fluorescence lifetime values of HSA and HSA-Au/Ag NPs from time-resolved fluorescence spectroscopic analysis further authenticated the findings of steady-state emission measurements. The formation of HSA corona on the Au/Ag NPs surface was established on the basis of experimental quenching data and theoretical values. The occurrence of partial unfolding of HSA upon its interaction with the Au/Ag NPs surface was established by using an extrinsic fluorophore 1-anilino-8-naphthalenesulfonic acid (ANS). Absorption, Fourier transform infrared (FT-IR), Raman, circular dichroism (CD), and excitation-emission matrix (3D) spectral studies were also carried out to explore Au/Ag NPs-induced tertiary and secondary conformational changes of HSA. The influence of Au/Ag NPs on the esterase-like activity of HSA was established by probing the hydrolysis of p-nitrophenyl acetate.
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