在象在不同 pH 价值的条件下面的牛的浆液白朊和免疫球蛋白 G 那样的金 nanoparticles 和蛋白质之间的相互作用基于在蛋白质与金 nanoparticles 是固定的前后,蛋白质熄灭的希腊语的第六个字母潜力和荧光的测量被学习。聚集被 TEM 描述和紫外力的光谱学决心在蛋白质的增加以后在金胶体发现水的答案。结果证明希腊语的第六个字母潜力的价值是相当不同的,有约束力的经常的 Kb 和 stoichiometry n 稍微随 pH 的增加被增加价值。在结论,二个因素能显著地影响在金 nanoparticles 和蛋白质之间的相互作用,也就是说,在金 nanoparticles 和吲哚之间的表面充电和协作效果蛋白质的色氨酸残余组织。
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.