Native Laser Lithography of His-Tagged Proteins by Uncaging of Multivalent Chelators

被引：34

作者：

Bhagawati, Maniraj ^{[1
,2
,3
]}

Lata, Suman ^{[2
,3
]}

Tampe, Robert ^{[2
,3
]}

Piehler, Jacob ^{[1
,2
,3
]}

机构：

[1] Univ Osnabruck, Div Biophys, D-49076 Osnabruck, Germany

[2] Goethe Univ Frankfurt, Cluster Excellence CEF Macromol Complexes, D-60438 Frankfurt, Germany

[3] Goethe Univ Frankfurt, Inst Biochem, D-60438 Frankfurt, Germany

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2010年 / 132卷 / 17期

关键词：

FUNCTIONAL IMMOBILIZATION; MOTOR PROTEINS; SURFACES; STREPTAVIDIN; BIOMOLECULES; BIOTIN;

D O I：

10.1021/ja1000714

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We report a generic approach for targeting proteins into micropatterns by in situ laser Lithography. To this end, we have designed a photocleavable oligohistidine peptide for caging tris(nitrilo triacetic acid) (tris-NTA) groups on surfaces by multivalent interactions. Local photofragmentation of the peptide by UV illumination through a photomask or by a confocal laser beam uncages tris-NTA, thus generating free binding sites for rapid, site-specific capturing of His-tagged proteins into micropatterns. Iterative writing of proteins by laser lithography enabled for assembly of multiplexed functional protein microstructures on surfaces. Thus, versatile, user-defined protein micropatterns can be assembled under physiological conditions with a standard confocal laser-scanning microscope.

引用

页码：5932 / +

页数：3

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