Native laser lithography of his-tagged proteins by uncaging of multivalent chelators

S Lata, M Bhagawati, R Tampé, J Piehler

Research output: Contribution to journalArticle (Academic Journal)peer-review

32 Citations (Scopus)

Abstract

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.
Translated title of the contributionNative laser lithography of his-tagged proteins by uncaging of multivalent chelators
Original languageEnglish
Pages (from-to)5932 - 5933
Number of pages2
JournalJournal of the American Chemical Society
Volume132 (17)
DOIs
Publication statusPublished - May 2010

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