期刊
LANGMUIR
卷 26, 期 9, 页码 6097-6101出版社
AMER CHEMICAL SOC
DOI: 10.1021/la904829y
关键词
-
资金
- German Research Foundation (DFG)
The site-selective, oriented, covalent immobilization of proteins on surfaces is an important issue in the establishment of microarrays, biosensors, biocatalysts, and cell assays. Here we describe the preparation of self-assembled monolayers consisting of benzylguanine thiols (BGT) to which SNAP-tag fusion proteins can be covalently linked. The SNAP-tag, a modified O-6-alkylguanine-DNA alkyltransferase (AGT). reacts with the headgroup of BGT and becomes covalently bound upon the release of guanine. Bacterially produced recombinant His-tag-SNAP-tag-GFP was used to demonstrate the site-specific immobilization on BGT surface patterns created by microcontact printing (mu CP). With this versatile method, any SNAP-tag protein can be coupled to a surface.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据