Benzylguanine Thiol Self-Assembled Mono layers for the Immobilization of SNAP-tag Proteins on Microcontact-Printed Surface Structures

被引：42

作者：

Engin, Sinem ^{[1
]}

Trouillet, Vanessa ^{[2
]}

Franz, Clemens M. ^{[1
]}

Welle, Alexander ^{[3
]}

Bruns, Michael ^{[2
]}

Wedlich, Doris ^{[1
]}

机构：

[1] KIT, Ctr Funct Nanostruct, D-76131 Karlsruhe, Germany

[2] KIT, Inst Mat Res 3, D-76131 Karlsruhe, Germany

[3] KIT, Inst Biol Interfaces, D-76131 Karlsruhe, Germany

来源：

LANGMUIR | 2010年 / 26卷 / 09期

关键词：

PHOTOELECTRON-SPECTROSCOPY; SELECTIVE IMMOBILIZATION; FUSION PROTEINS; SMALL-MOLECULE; LIVING CELLS; XPS-ANALYSIS; COVALENT; FILMS; GOLD; MICROARRAYS;

D O I：

10.1021/la904829y

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

页码：6097 / 6101

页数：5

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