Geoinspired synthetic chrysotile, which represents an ideal asbestos reference standard, has been utilized to investigate homornolecularexchange 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 coatin-extent. Circular dichroism spectroscopy has been used to investigate the adsorpti on/desorpt ion equilibriurn 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 differcut bindina 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 inimicking the behavior of asbestos fibers and allows to better understand their interaction with a biolouical environment. (c) 2007 Elsevier Inc. All rights reserved.