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

被引：56

作者：

Hwang, Dong Soo ^{[1
]}

Harrington, Matthew J. ^{[2
]}

Lu, Qingye ^{[3
]}

Masic, Admir ^{[2
]}

Zeng, Hongbo ^{[3
]}

Waite, J. Herbert ^{[4
]}

机构：

[1] Pohang Univ Sci & Technol, POSTECH Ocean Sci & Technol Inst, Pohang 790784, South Korea

[2] Max Planck Inst Colloids & Interfaces, Dept Biomat, D-14424 Potsdam, Germany

[3] Univ Alberta, Dept Chem Engn, Edmonton, AB T6G 2M7, Canada

[4] Univ Calif Santa Barbara, Mat Res Lab, Santa Barbara, CA 93106 USA

来源：

JOURNAL OF MATERIALS CHEMISTRY | 2012年 / 22卷 / 31期

基金：

加拿大自然科学与工程研究理事会; 新加坡国家研究基金会;

关键词：

MYTILUS-EDULIS; ADHESIVE PROTEIN; AQUEOUS-SOLUTION; CATECHOL; DOPA; COATINGS; ANATASE; FILMS; NANOPARTICLES; COMPLEXATION;

D O I：

10.1039/c2jm32439c

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

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 TiO2-protein 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.

引用

页码：15530 / 15533

页数：4

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