摘要
The interaction between gold nanoparticles and proteins such as bovine serum albumin and immunoglobulin G under the condition of different pH values was studied based on the measurement of zeta potential and fluorescence quenching of the proteins before and after proteins were bound with gold nanoparticles. Aggregations were found in gold colloid aqueous solution after addition of proteins by TEM characterization and UV-Vis spectroscopy deterruination. The results showed that the values of zeta potential were quite different, the binding constant Kb and stoichiometry n were slightly increased with the increase of pH value. In conclusion, two factors could affect markedly the interaction between gold nanoparticles and proteins, that is, surface charge and the coordination effect between gold nanoparticles and indole group of the tryptophan residue of proteins.
The interaction between gold nanoparticles and proteins such as bovine serum albumin and immunoglobulin G under the condition of different pH values was studied based on the measurement of zeta potential and fluorescence quenching of the proteins before and after proteins were bound with gold nanoparticles. Aggregations were found in gold colloid aqueous solution after addition of proteins by TEM characterization and UV-Vis spectroscopy deterruination. The results showed that the values of zeta potential were quite different, the binding constant Kb and stoichiometry n were slightly increased with the increase of pH value. In conclusion, two factors could affect markedly the interaction between gold nanoparticles and proteins, that is, surface charge and the coordination effect between gold nanoparticles and indole group of the tryptophan residue of proteins.
基金
Project supported by the National Natural Science Foundation of China （No. 30471599） and Development Foundation of Shanghai Science and Technology （No.03ZR14057）.
