The increasing interest in nanoscience and technology arises from its valuable applications in the manufacturing, health and energy fields. This research project is focused on understanding the interactions of Super Paramagnetic Iron(III) Oxide Nanoparticles (SPIONs) with human serum fibrinogen and the effects of protein oxidation on their binding affinity. Spectroscopic methods were used to determine the binding constant (Ka), enthalpy changes (?H?), entropy changes (?S?), and free energy changes (?G?). The results suggest that the interaction was spontaneous and that electrostatic interactions played key roles in the binding process. The fluorescence quenching constants (KSV) determined at different temperatures (1.87x10-6 M-1, and 1.46x10-6 M-1 at 300 K and 320 K, respectively) indicated that SPIONs quenched fibrinogen fluorescence mainly by a static quenching mechanism. Oxidation of the fibrinogen showed a significant decrease in binding constants and an adverse correlation was established between increasing carbonyl concentrations and decreasing binding constants.

Effects of oxidation on the interactions of human serum fibrinogen and super paramagnetic iron(III) oxide nanoparticles

243rd National Meeting (2012)

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