Self-assembly of flagellin on Au(111) surfaces

•Flagellin from Pseudomonas fluorescens was immobilized on Au(111).•Flagellin monomers spontaneously self-assemble forming a monolayer thick film.•The protein assembles as cylindrical-like structures containing 4–6 units of flagellin.•The films are conductive and allow allocation of electrochemicall...

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Bibliographic Details
Published in:Journal of colloid and interface science 2014-11, Vol.433, p.86-93
Main Authors: González Orive, Alejandro, Pissinis, Diego E., Diaz, Carolina, Miñán, Alejandro, Benítez, Guillermo A., Rubert, Aldo, Daza Millone, Antonieta, Rumbo, Martin, Hernández Creus, Alberto, Salvarezza, Roberto C., Schilardi, Patricia L.
Format: Article
Language:English
Subjects:
Cytochrome C
Flagellin
Flagellin - chemistry
Gold - chemistry
Membranes, Artificial
Metal Nanoparticles - chemistry
Protein adsorption
Protein Multimerization
Pseudomonas fluorescens - chemistry
Self-assembly
Surface Plasmon Resonance - methods
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Summary:•Flagellin from Pseudomonas fluorescens was immobilized on Au(111).•Flagellin monomers spontaneously self-assemble forming a monolayer thick film.•The protein assembles as cylindrical-like structures containing 4–6 units of flagellin.•The films are conductive and allow allocation of electrochemically active Cyt C. The adsorption of flagellin monomers from Pseudomonas fluorescens on Au(111) has been studied by Atomic Force Microscopy (AFM), Scanning Tunneling Microscopy (STM), X-ray Photoelectron Spectroscopy (XPS), Surface Plasmon Resonance (SPR), and electrochemical techniques. Results show that flagellin monomers spontaneously self-assemble forming a monolayer thick protein film bounded to the Au surface by the more hydrophobic subunit and exposed to the environment the hydrophilic subunit. The films are conductive and allow allocation of electrochemically active cytochrome C. The self-assembled films could be used as biological platforms to build 3D complex molecular structures on planar metal surfaces and to functionalize metal nanoparticles.
ISSN:0021-9797
1095-7103
DOI:10.1016/j.jcis.2014.07.016