Kwant Richard L, Jaffe Jake, Palmere Peter J, Francis Matthew B
Department of Chemistry , University of California at Berkeley , Berkeley , California 94720-1460 , USA . Email:
Materials Sciences Division , Lawrence Berkeley National Laboratory , Berkeley , California 94720 , USA.
Chem Sci. 2015 Apr 16;6(4):2596-2601. doi: 10.1039/c4sc03790a. Epub 2015 Feb 27.
Synthetically modified proteins are increasingly finding applications as well-defined scaffolds for materials. In practice it remains difficult to construct bioconjugates with precise levels of modification because of the limited number of repeated functional groups on proteins. This article describes a method to control the level of protein modification in cases where there exist multiple potential modification sites. A protein is first tagged with a handle using any of a variety of modification chemistries. This handle is used to isolate proteins with a particular number of modifications affinity chromatography, and then the handle is elaborated with a desired moiety using an oxidative coupling reaction. This method results in a sample of protein with a well-defined number of modifications, and we find it particularly applicable to systems like protein homomultimers in which there is no way to discern between chemically identical subunits. We demonstrate the use of this method in the construction of a protein-templated light-harvesting mimic, a type of system which has historically been difficult to make in a well-defined manner.
合成修饰的蛋白质越来越多地被用作定义明确的材料支架。实际上，由于蛋白质上重复官能团的数量有限，构建具有精确修饰水平的生物共轭物仍然很困难。本文描述了一种在存在多个潜在修饰位点的情况下控制蛋白质修饰水平的方法。首先使用多种修饰化学方法中的任何一种用一个手柄标记蛋白质。这个手柄用于通过亲和色谱法分离具有特定修饰数量的蛋白质，然后使用氧化偶联反应将手柄用所需的部分进行修饰。该方法产生具有明确修饰数量的蛋白质样品，我们发现它特别适用于像蛋白质同多聚体这样无法区分化学上相同亚基的系统。我们展示了该方法在构建蛋白质模板光捕获模拟物中的应用，这种系统在历史上一直难以以明确的方式制备。
Zotero 插件
