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Effect of Surface Hydrophobicity on the Function of the Immobilized Biomineralization Protein Mms6

TitleEffect of Surface Hydrophobicity on the Function of the Immobilized Biomineralization Protein Mms6
Publication TypeJournal Article
Year of Publication2015
AuthorsLiu, XP, Zhang, HH, Nayak, S, Parada, G, Anderegg, J, Feng, SR, Nilsen-Hamilton, M, Akinc, M, Mallapragada, SK
Journal Engineering Chemistry Research
Date Published10
Type of ArticleArticle
ISBN Number0888-5885
Accession NumberWOS:000363917000016
Keywordsadsorption, Biomedical applications, functionalization, gold, iron-binding, magnetosome formation, magnetotactic bacterium, multifunctional magnetic nanoparticles, nanocrystals, nanostructures

es close to those seen in nature, in contrast to its behavior on more hydrophilic surfaces. We propose that this hydrophobicity effect might be due to the amphiphilic nature of the Mms6 protein and its tendency to incorporate the hydrophobic N-terminal domain into the hydrophobic lipid bilayer environment of the magnetosome membrane, exposing the hydrophilic C-terminal domain that promotes biomineralization. Supporting this hypothesis, the larger and well-formed magnetite nanoparticles were found to be preferentially located on ODT surfaces covered with Mms6 as compared to control samples, as characterized by scanning electron microscopy, X-ray diffraction, X-ray photoelectron spectroscopy, and atomic force microscopy studies. A C-terminal domain mutant of this protein did not form the same network structure as wild-type Mms6, suggesting that the network structure is important for the magnetite nanocrystal formation. This study provides valuable insights into the role of surface hydrophilidty on the action of the biomineralization protein Mms6 to synthesize magnetic nanocrystals and provides a facile route to controlling bioinspired nanocrystal synthesis in vitro.

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Bioinspired Materials