The aim of this work is to get insight into adsorption-induced changes in the protein stability, as well as into mechanism of binding interaction of one of the most abundant plasma protein, namely BSA (Bovine serum albumin, fraction V) with two representative nanomaterials, i.e. titanium dioxide (TiO2 JRCNM01005a, rutileanatase, 15-24 nm)[1] and silica (SiO2 JRCNM02002a, synthetic amorphous, 14-23 nm)[2]. NanoDSC TA Instruments was used for the evaluation of the protein thermal stability represented by heat capacity change (∆Cp), denaturation temperature (Tpeak), denaturation enthalpy (∆Hd) and entropy (∆Sd) of the bound proteins in the BSA/TiO2 and BSA/SiO2 systems. The main binding thermodynamic parameters driving the interaction in the protein-NPs systems, namely the binding constant K and stoichiometry n, binding enthalpy ΔH, Gibbs energy ΔG and entropy ΔS changes were obtained using Isothermal Titration Calorimetry (Microcal iTC200 microcalorimeter). The results allow for a better understanding of the driving forces controlling the proteins/nanoparticles interaction involved in different biological processes.