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

Show full item record

Page view(s)

4
Last Week
0
Last month
0
checked on Mar 4, 2024

Google ScholarTM

Check

Altmetric