Interaction of γ-Fe2O3 nanoparticles with fibrinogen

In this article, an attempt is made to analysis the binding mechanism of gamma-Fe2O3 nanoparticles with fibrinogen by using a combination of circular dichroism, UV-vis, fluorescence spectroscopic and computational methods. The multi-spectroscopic data revealed that the complex easily formed between gamma-Fe2O3 nanoparticles and fibrinogen by mainly hydrogen bonding forces. The binding constants of fibrinogen with gamma-Fe2O3 nanoparticles were 2.24 x 10(7), 1.15 x 10(7) and 0.72 x 10(7) L mol(-1) at 298, 304, and 310 K, respectively. Furthermore, the results from circular dichroism, UV-vis, synchronous fluorescence, and three-dimensional fluorescence studies showed that the strong binding interaction of gamma-Fe2O3 nanoparticles with fibrinogen induced an obvious perturbation in the protein secondary and tertiary structure. Moreover, the results of molecular modeling indicated the existence of the preferable binding site on fibrinogen for gamma-Fe2O3 NPs model. (C) 2015 Elsevier B.V. All rights reserved.