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Effect of Surface Hydrophobicity on the Function of the Immobilized Biomineralization Protein Mms6
Author(s) -
Xunpei Liu,
Honghu Zhang,
Srikanth Nayak,
German Alberto Parada,
James W. Anderegg,
Shuren Feng,
Marit NilsenHamilton,
Müfit Akinç,
Surya K. Mallapragada
Publication year - 2015
Publication title -
industrial and engineering chemistry research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.878
H-Index - 221
eISSN - 1520-5045
pISSN - 0888-5885
DOI - 10.1021/acs.iecr.5b01413
Subject(s) - biomineralization , magnetotactic bacteria , magnetosome , magnetite , nanocrystal , chemical engineering , amphiphile , nanoparticle , materials science , bilayer , chemistry , crystallography , nanotechnology , membrane , organic chemistry , biochemistry , polymer , copolymer , engineering , metallurgy
Magnetotactic bacteria produce magnetic nanocrystals with uniform shapes and sizes in nature, which has inspired in vitro synthesis of uniformly sized magnetite nanocrystals under mild conditions. Mms6, a biomineralization protein from magnetotactic bacteria with a hydrophobic N-terminal domain and a hydrophilic C-terminal domain, can promote formation of magnetite nanocrystals in vitro with well-defined shape and size in gels under mild conditions. Here we investigate the role of surface hydrophobicity on the ability of Mms6 to template magnetite nanoparticle formation on surfaces. Our results confirmed that Mms6 can form a protein network structure on a monolayer of hydrophobic octadecanethiol (ODT)-coated gold surfaces and facilitate magnetite nanocrystal formation with uniform sizes 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...

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