Interaction of colloidal AgTiO2 nanoparticles with bovine serum albumin

The interaction between colloidal AgTiO2 nanoparticles and bovine serum albumin (BSA) was studied by using absorption, steady state, time resolved and synchronous fluorescence spectroscopy measurements. Absorption spectroscopy proved the formation of a ground state BSA⋯AgTiO2 complex. Upon excitation of BSA, colloidal AgTiO2 nanoparticles effectively quenched the intrinsic fluorescence of BSA. The number of binding sites (n = 1.06) and apparent binding constant (K = 3.71 × 105 M−1) were calculated by the fluorescence quenching method. A static mechanism and conformational changes of BSA were observed.

The interaction between colloidal AgTiO2 nanoparticles and bovine serum albumin (BSA) has been studied by absorption, steady state, time resolved and synchronous fluorescence spectroscopic techniques. The quenching rate constant, binding constant and number of binding sites were calculated according to the relevant fluorescence quenching data. From the synchronous fluorescence spectra, it can be shown that the conformational change of BSA is induced by the interaction of colloidal AgTiO2 nanoparticles with the tyrosine micro-region of BSA molecules. This study is expected to provide important insight in the interactions of physiologically important protein BSA with metal nanoparticles.Figure optionsDownload as PowerPoint slide