Probing the interaction between niobium pentoxide nanoparticles and serum albumin proteins by Spectroscopic approaches.

Nanoparticles (NPs) can directly or indirectly enter into the body because of their small size; then they tend to alter the conformation and function of proteins upon interaction with them. Thus, it is crucial to understand the impact of NPs in a biological medium. Recently, niobium pentoxide nanoparticles (NbO NPs) are finding increasing applications in the biological system, for example, bone tissue and dental material, matrix for biosensing of proteins, . In all such applications, the NbO NP interacts with proteins and other biomolecules. Hence, the study of such interactions is of considerable importance. Here in this work, we present the impact of NbO NP on the structure, stability and activity of blood proteins, bovine serum albumin (BSA) and human serum albumin (HSA) by means of various spectroscopic approaches. Steady-state fluorescence studies indicated that intrinsic fluorescence intensities of both serum albumin proteins got quenched upon their interaction with NP. The nature of the quenching was elucidated by time-resolved fluorescence and absorption measurements. Using circular dichroism (CD) and synchronous fluorescence spectroscopy (SFS), the structural perturbations of the protein molecules after interaction with NP were investigated. Moreover, the role of temperature on protein stability upon complexation with NP was also explored. In addition, the effect of NP on protein functionality was probed by esterase-like activity assays.Communicated by Ramaswamy H. Sarma.