Consequently, is primordial to find out a model that is able to account for these interactions most efficiently in a qualitative as well as a quantitative way. Concerning the biomineralization process several works suggest that BSA inhibit the hydroxyapatite

formation when apatite is precipitated in a medium containing the protein [10] and [11]. Mueller and Sikes [12] suggested that there are biomineralization inhibitors that affect the nucleation and crystal growth of apatite. In the first case the biomolecules could bind to the ions present in simulated biological fluid by sequestering lattice Atezolizumab ions therefore reducing ion activity and inhibiting nucleation. In the second case the biomolecules affect the crystal growth by binding to crystal

surfaces rather than ions present in simulated biological fluid. Conversely, Marques et al. [11] increased the carbonate content of simulated inorganic plasma containing BSA (CSIPA) causing a higher mineralization on calcium phosphate ceramics and bioglass substrates when compared with simulated body fluid containing BSA (SBFA). In general, the effect of albumin on hydroxyapatite crystallization has been studied by the addition of BSA into aqueous selleck media or simulated body fluid containing calcium and phosphate. In these cases the protein is widely dispersed in the medium where apatite crystals are forming. However, few works studied in detail the precipitation of calcium phosphates onto wide surfaces where BSA was previously adsorbed. In this work we investigated the kinetics of BSA adsorption onto apatite surface and the conditions where mono and multilayers of proteins are formed. This study also focused on the

Molecular motor characterization of the calcium phosphate layer (CP) precipitated onto HA surface previously coated with a film of BSA, after the immersion in simulated body fluid (SBF) for 7 days. The role of BSA on hydroxyapatite bioactivity is discussed. Hydroxyapatite (HA) was synthesized via wet method as described elsewhere [13]. The powder was uni-axially pressed at 30 KN into discs with diameter of 10 mm and thickness of 1 mm. These samples were then sintered with a temperature increment of 10 °C s−1 until reaching 1000 °C and left during 2 hours at this temperature. Bovine serum albumin (BSA) a well-characterized protein with a molecular weight of 69 kDa, isoelectric point of 4.9 (14) and dimensions of 14.0 nm × 4.0 nm [15] was obtained from the Sigma Chemical Co. (A7638, crystallized and lyophilized). BSA structure contains 70% of α helix and 15% of β sheet [16]. The HA sample had a Ca/P ratio of 1.67 ± 0.03, which was measured by X-Fluorescence and specific surface area of 45 ± 5 m2 measured by BET method. Conventional X-ray diffraction was used to characterize hydroxyapatite powder samples.