Anchoring of Histidine-Tagged Proteins to Molecular Printboards: Self-assembly, Thermodynamic Modeling, and Patterning

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Ludden, Manon J.W. and Mulder, Alart and Schulze, Katrin and Subramaniam, Vinod and Tampe, Robert and Huskens, Jurriaan (2008) Anchoring of Histidine-Tagged Proteins to Molecular Printboards: Self-assembly, Thermodynamic Modeling, and Patterning. Chemistry: a European Journal, 14 (7). pp. 2044-2051. ISSN 0947-6539

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Abstract:In this paper the multivalent binding of hexahistidine (His6)-tagged proteins to β-cyclodextrin (β-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 Ni4 in 1:1 stoichiometry. On the surface, however, the majority of His6-MBP was complexed to surface-immobilized β-CDs through three Ni4 complexes. This difference is explained by the high effective β-CD concentration at the surface and is a new example of supramolecular interfacial expression. In a similar adsorption scheme, SPR proved that the α-proteasome could be attached to β-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 Ni4. Fluorescence measurements showed that the (His6)4-DsRed-FT is bound strongly through Ni4 to the molecular printboard.
Item Type:Article
Copyright:© 2008 Wiley InterScience
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Science and Technology (TNW)
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Link to this item:http://purl.utwente.nl/publications/72208
Official URL:http://dx.doi.org/10.1002/chem.200701478
Dataset URL:http://www.wiley-vch.de/contents/jc_2111/2008/f701478_s.pdf
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