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Protein-Protein Interactions in Reversibly Assembled Nanopatterns
Department of Functional Nanomaterials, Institute of Physics, Savanoriu¸ 231, LT-02300 Vilnius, Lithuania.
Department of Functional Nanomaterials, Institute of Physics, Savanoriu¸ 231, LT-02300 Vilnius, Lithuania.
Institute of Biochemistry and Cluster of Excellence Macromolecular Complexes (CEF), Johann Wolfgang Goethe-University, Max-von-Laue-Strasse 9, 60438 Frankfurt, Germany.
Institute of Biochemistry and Cluster of Excellence Macromolecular Complexes (CEF), Johann Wolfgang Goethe-University, Max-von-Laue-Strasse 9, 60438 Frankfurt, Germany.
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2008 (English)In: Nano letters (Print), ISSN 1530-6984, E-ISSN 1530-6992, Vol. 8, no 10, 3369-3375 p.Article in journal (Refereed) Published
Abstract [en]

We describe herein a platform to study protein-protein interactions and to form functional protein complexes in nanoscopic surface domains. For this purpose, we employed multivalent chelator (MCh) templates, which were fabricated in a stepwise procedure combining dip-pen nanolithography (DPN) and molecular recognition-directed assembly. First, we demonstrated that an atomic force microscope (AFM) tip inked with an oligo(ethylene glycol) (OEG) disulfide compound bearing terminal biotin groups can be used to generate biotin patterns on gold achieving line widths below 100 nm, a generic platform for fabrication of functional nanostructures via the highly specific biotin-streptavidin recognition. Subsequently, we converted such biotin/streptavidin patterns into functional MCh patterns for reversible assembly of histidine- tagged (His-tagged) proteins via the attachment of a tris-nitriloacetic acid (trisNTA) biotin derivative. Fluorescence microscopy confirmed reversible immobilization of the receptor subunit ifnar2-His10 and its interaction with interferon-a2 labeled with fluorescent quantum dots in a 7 × 7 dot array consisting of trisNTA spots with a diameter of ~230 nm. Moreover, we carried out characterization of the specificity, stability, and reversibility as well as quantitative real-time analysis of protein-protein interactions at the fabricated nanopatterns by imaging surface plasmon resonance. Our work offers a route for construction and analysis of functional protein-based nanoarchitectures. © 2008 American Chemical Society.

Place, publisher, year, edition, pages
2008. Vol. 8, no 10, 3369-3375 p.
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Natural Sciences
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URN: urn:nbn:se:liu:diva-50131DOI: 10.1021/nl801892mOAI: oai:DiVA.org:liu-50131DiVA: diva2:271027
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2017-12-12

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