Fatty acid transfer between serum albumins and shungite carbon nanoparticles and its effect on protein aggregation and association.

Abstract

The bioactivity of the natural ultrafine carbon form shungite nanocarbon (ShC) is of particular interest both for biomedical applications of such nanomaterials and their negative impact on the aquatic environmental. Here we studied the interaction of serum albumin (SA) with ShC nanoparticles in aqueous dispersion with respect to its structural-dynamic, thermodynamic, and hydrodynamic effects. Electron spin resonance (EPR) with a 5-DOXYL-stearic acid spin probe (5DSA) demonstrates that ShC can affect fatty acid (FA) binding by SA, protein conformation in the stearic FA spin probe binding region, and protein aggregation due to the partial transfer of FA to the ShC nanoparticles. The ratio of SA fractions changes in the presence of ShC in favor of the fraction that is less saturated with FA as shown by differential scanning calorimetry (DSC). The stability of interaction with ShC is significantly higher for aggregates of SA molecules that carry physiological amounts of FA, compared to aggregates of the FA-free protein, as studied by dynamic light scattering (DLS) analysis. Generally, the mixed dispersion of SA and ShC nanoparticles is more homogeneous than the SA solution alone. This is manifested both in the size of the molecular associates and in the microenvironment of the protein-bound FA. The formation of the SA-ShC interface is likely to result in a greater uniformity of the FA binding sites and a decrease in protein fractions and "hot patches" on the protein surface responsible for the supramolecular heterogeneity of the protein in solution.