Synthesis of ZnO nanoparticles and conjugation study with Bovine Serum Albumin

LEDESMA, A. E

Bahía Blanca

Congreso; XLIII Reunión Anual de la Sociedad Argentina de Biofísica; 2014

The interaction of nanoparticles (NPs) with biological fluids may induce conformational changes in the proteins present in the medium. Such interaction could induce function loss or important modification in some proteins. The interaction between Bovine Serum Albumin (BSA) with semiconductor zinc oxide (ZnO) NPs, synthetized by aqueous route from zinc nitrate hexahydrate, was studied using spectroscopy of absorption, fluorescence, Fourier Transform Infrared and Raman. The addition of ZnO NPs quenched the intrinsic fluorescence of BSA. The Raman spectra confirm the interaction of the Trp and Tyr residues on surface of NP, while that the FTIR results indicate that the metal oxide surface induce conformational changes where the main transformation is a change in α-helix (∼ 9 %) and an increasing in β-sheet structures (∼ 25 %). At high NPs concentration, with the increment of BSA concentration a blue shift in λmax absorption of protein was observed, which confirm the conformational changes in the protein. On the other hand, a decreasing of absorbance and emition of ZnO NPs was observed by its interaction with BSA. This protein contributed at the stabilization and bioconjugation of ZnO NPs reducing the aggregation in solution