| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1230051 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2015 | 8 Pages |
•Binding interactions of γ-Fe2O3 nanoparticles with fibrinogen were investigated.•Strong interaction exists between γ-Fe2O3 nanoparticles and fibrinogen.•γ-Fe2O3 nanoparticles binding effect the secondary and tertiary structures of fibrinogen.•Hydrogen bonding forces stabilize the γ-Fe2O3 nanoparticles–fibrinogen complex.
In this article, an attempt is made to analysis the binding mechanism of γ-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 γ-Fe2O3 nanoparticles and fibrinogen by mainly hydrogen bonding forces. The binding constants of fibrinogen with γ-Fe2O3 nanoparticles were 2.24 × 107, 1.15 × 107 and 0.72 × 107 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 γ-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 γ-Fe2O3 NPs model.
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