Anchoring of histidine-tagged proteins to molecular printboards: self-assembly, thermodynamic modeling, and patterning

Manon J W Ludden, Alart Mulder, Katrin Schulze, Vinod Subramaniam, Robert Tampé, Jurriaan Huskens

    Research output: Contribution to JournalArticleAcademicpeer-review


    In this paper the multivalent binding of hexahistidine (His6)-tagged proteins to beta-cyclodextrin (beta-CD) self-assembled monolayers (SAMs) by using the nickel(II) complex of a hetero-divalent orthogonal adamantyl nitrilotriacetate linker (4) is described. Nonspecific interactions were suppressed by using monovalent adamantyl-hexa(ethylene glycol) derivative 3. With the mono-His6-tagged maltose binding protein (His6-MBP), thermodynamic modeling based on surface plasmon resonance (SPR) titration data showed that the MBP molecules in solution were linked, on average, to Ni.4 in 1:1 stoichiometry. On the surface, however, the majority of His(6)-MBP was complexed to surface-immobilized beta-CDs through three Ni.4 complexes. This difference is explained by the high effective beta-CD concentration at the surface and is a new example of supramolecular interfacial expression. In a similar adsorption scheme, SPR proved that the alpha-proteasome could be attached to beta-CD SAMs in a specific manner. Patterning through microcontact printing of (His6)4-DsRed-fluorescent timer (DsRed-FT), which is a tetrameric, visible autofluorescent protein, was carried out in the presence of Ni.4 Fluorescence measurements showed that the (His6)4-DsRed-FT is bound strongly through Ni.4 to the molecular printboard.

    Original languageEnglish
    Pages (from-to)2044-51
    Number of pages8
    JournalChemistry: A European Journal
    Issue number7
    Publication statusPublished - 2008


    • Adsorption
    • Binding Sites
    • Carrier Proteins
    • Histidine
    • Luminescent Proteins
    • Maltose-Binding Proteins
    • Models, Chemical
    • Molecular Conformation
    • Nickel
    • Nitrilotriacetic Acid
    • Organometallic Compounds
    • Particle Size
    • Proteasome Endopeptidase Complex
    • Surface Plasmon Resonance
    • Surface Properties
    • Thermodynamics
    • Time Factors
    • beta-Cyclodextrins
    • Journal Article
    • Research Support, Non-U.S. Gov't


    Dive into the research topics of 'Anchoring of histidine-tagged proteins to molecular printboards: self-assembly, thermodynamic modeling, and patterning'. Together they form a unique fingerprint.

    Cite this