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

TitleMussel foot protein-1 (mcfp-1) interaction with titania surfaces().
Publication TypeJournal Article
Year of Publication2012
AuthorsHwang, DSoo, Harrington, MJ, Lu, Q, Masic, A, Zeng, H, Waite, JH
JournalJ Mater Chem
Date Published2012 Aug 21

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).

Alternate JournalJ Mater Chem
PubMed ID23100857
PubMed Central IDPMC3478952
Grant ListR01 DE018468 / DE / NIDCR NIH HHS / United States