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Issue 31, 2012
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Mussel foot protein-1 (mcfp-1) interaction with titania surfaces

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Marine mussels utilize a variety of DOPA-rich proteins for purposes of underwater adhesion, as well as for creating hard and flexible surface coatings for their tough and stretchy byssal fibers. In the present study, moderately strong, yet reversible wet adhesion between the protective mussel coating protein, mcfp-1, and amorphous titania was measured with a surface force apparatus (SFA). In parallel, resonance Raman spectroscopy was employed to identify the presence of bidentate DOPA–Ti coordination bonds at the TiO2protein interface, suggesting that catechol–TiO2 complexation contributes to the observed reversible wet adhesion. These results have important implications for the design of protective coatings on TiO2.

Graphical abstract: Mussel foot protein-1 (mcfp-1) interaction with titania surfaces

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The article was received on 19 Apr 2012, accepted on 25 Jun 2012 and first published on 25 Jun 2012

Article type: Communication
DOI: 10.1039/C2JM32439C
Citation: J. Mater. Chem., 2012,22, 15530-15533
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    Mussel foot protein-1 (mcfp-1) interaction with titania surfaces

    D. S. Hwang, M. J. Harrington, Q. Lu, A. Masic, H. Zeng and J. H. Waite, J. Mater. Chem., 2012, 22, 15530
    DOI: 10.1039/C2JM32439C

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