Native Laser Lithography of His-Tagged Proteins by Uncaging of Multivalent Chelators
Autor(en): | Bhagawati, Maniraj Lata, Suman Tampe, Robert Piehler, Jacob |
Stichwörter: | BIOMOLECULES; BIOTIN; Chemistry; Chemistry, Multidisciplinary; FUNCTIONAL IMMOBILIZATION; MOTOR PROTEINS; STREPTAVIDIN; SURFACES | Erscheinungsdatum: | 2010 | Herausgeber: | AMER CHEMICAL SOC | Journal: | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | Volumen: | 132 | Ausgabe: | 17 | Startseite: | 5932+ | Zusammenfassung: | 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. |
ISSN: | 00027863 | DOI: | 10.1021/ja1000714 |
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geprüft am 25.04.2024