Synthetic chrysotile nanocrystals as a reference standard to investigate surface-induced serum albumin structural modifications

Geoinspired synthetic chrysotile, which represents an ideal asbestos reference standard, has been utilized to investigate homomolecular exchange of bovine serum albumin (BSA), the major plasma protein, between the adsorbed and dissolved state at the interface between asbestos fibers and biological medium. FTIR spectroscopy has been used to quantify BSA structural modifications due to surface adhesion on chrysotile fibers as a function of the surface coating extent. Circular dichroism spectroscopy has been used to investigate the adsorption/desorption equilibrium through analysis of the BSA structural perturbations after protein desorption from chrysotile surface. Data results show clearly that in the solid state BSA modifications are driven by surface interaction with the substrate, following a bimodal adsorption evidenced by two different binding constants. On the other hand, BSA desorbed in solution is able to rearrange, in the lack of substrate, although keeping irreversible modifications with respect to the native species. The lack of regaining its native structure certainly affects albumin interaction with biological environment. The present investigation on the stoichiometric synthetic geoinspired chrysotile nanocrystals is the first approach toward a deeper attempt to use standard synthetic chrysotile reference samples in mimicking the behavior of asbestos fibers and allows to better understand their interaction with a biological environment.

Synthetic stoichiometric chrysotile nanofibers with constant structure and morphology have been first used as an ideal reference standard to define adsorption/desorption equilibrium of BSA. Irreversible protein unfolding has been quantified in the solid state and in the surnatant solutions as a function of the coating extent.Figure optionsDownload as PowerPoint slide