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Mussel foot protein-1 (mcfp-1) interaction with titania surfaces().

ABSTRACT: 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 TiO(2)-protein interface, suggesting that catechol-TiO(2) complexation contributes to the observed reversible wet adhesion. These results have important implications for the design of protective coatings on TiO(2).

SUBMITTER: Hwang DS

PROVIDER: S-EPMC3478952 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature

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Mussel foot protein-1 (mcfp-1) interaction with titania surfaces().

Hwang Dong Soo DS Harrington Matthew J MJ Lu Qingye Q Masic Admir A Zeng Hongbo H Waite J Herbert JH

Journal of materials chemistry 20120801 31

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 coordin ...[more]

PMID: 23100857

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