Post-polymerisation modification of surface chemical functionality and its effect on protein binding
作者:Cleo Choong、J. S. Foord、Jon-Paul Griffiths、Emily M. Parker、Luo Baiwen、Meghali Bora、Mark G. Moloney
DOI:10.1039/c2nj00002d
日期:——
Derivatisation of polystyrene by carbene insertions followed by diazonium coupling permits the introduction of diverse chemical functionality, providing access to materials with similar bulk properties, but in which surface chemical characteristics are systematically varied across a range of surface polarity, hydration and non-bonding interaction behaviour. Protein binding experiments with bovine serum albumin demonstrate that protein adhesion is dependent upon the identity of the surface chemical group, with tert-butyl, hexyl, dimethylamino, amino, and carboxyl modified systems all exhibiting higher levels of binding, while glycol, hydroxyl, and phosphonate give similar or lower levels of binding, relative to the control. This behaviour has been shown to be time dependent, and an approximate trend of protein binding with cheminformatic descriptors %PSA and contact angle was observed.
通过碳烯插入和重氮偶联对聚苯乙烯进行衍生,可以引入多种化学官能团,从而获得具有相似主体特性的材料,但其表面化学特性会在一系列表面极性、水合和非键相互作用行为中发生系统性变化。与牛血清白蛋白的蛋白质结合实验表明,蛋白质的粘附性取决于表面化学基团的特性,叔丁基、己基、二甲基氨基、氨基和羧基修饰系统都表现出较高的粘附性,而乙二醇、羟基和膦酸盐的粘附性与对照组相似或较低。这种行为已被证明与时间有关,并观察到蛋白质结合与化学信息描述符 %PSA 和接触角的近似趋势。