Abstract
In this study, the interaction of Fe3O4@CaAl-LDH@L-Dopa nanoparticles (NPs) with human serum albumin (HSA) was investigated in simulated physiological conditions applying UV-visible, fluorescence, and circular dichroism (CD) spectroscopic techniques. The consequences of UV-vis and CD spectroscopy demonstrated that the interaction of HSA to Fe3O4@CaAl-LDH@L-Dopa NPs enforced some conformational alterations within HSA. The fluorescence spectroscopy analysis indicated that by enhancing temperature, the Stern-Volmer quenching constant (Ksv) was decreased, which is relevant to a static quenching mechanism. The binding constant (Kb) was 7.07 × 104 M−1 while the number of the binding site (n) was 0.94 which is in compromise with its binding constant. Also, thermodynamic parameters (ΔH° > 0, ΔG° < 0, and ΔS° > 0) have suggested that hydrophobic forces perform a key role in the interaction of HSA with Fe3O4@CaAl-LDH@L-Dopa NPs. Displacement studies successfully carried out using the Warfarin and Ibuprofen have predicted that the binding of Fe3O4@CaAl-LDH@L-Dopa NPs to HSA is situated at site II (subdomain IIIA).
Communicated by Ramaswamy H. Sarma
Disclosure statement
The researchers state that they have no conflict of interest.
Funding
The Razi University Research Center's financial support is gratefully acknowledged.