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      Genetically-tunable mechanical properties of bacterial functional amyloid nanofibers

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      Author
      Abdelwahab, M. T.
      Kalyoncu, E.
      Onur, T.
      Baykara, M. Z.
      Seker U.O.S.
      Date
      2017
      Source Title
      Langmuir
      Print ISSN
      0743-7463
      Publisher
      American Chemical Society
      Volume
      33
      Issue
      17
      Pages
      4337 - 4345
      Language
      English
      Type
      Article
      Item Usage Stats
      118
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      147
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      Abstract
      Bacterial biofilms are highly ordered, complex, dynamic material systems including cells, carbohydrates, and proteins. They are known to be resistant against chemical, physical, and biological disturbances. These superior properties make them promising candidates for next generation biomaterials. Here we investigated the morphological and mechanical properties (in terms of Young’s modulus) of genetically-engineered bacterial amyloid nanofibers of Escherichia coli (E. coli) by imaging and force spectroscopy conducted via atomic force microscopy (AFM). In particular, we tuned the expression and biochemical properties of the major and minor biofilm proteins of E. coli (CsgA and CsgB, respectively). Using appropriate mutants, amyloid nanofibers constituting biofilm backbones are formed with different combinations of CsgA and CsgB, as well as the optional addition of tagging sequences. AFM imaging and force spectroscopy are used to probe the morphology and measure the Young’s moduli of biofilm protein nanofibers as a function of protein composition. The obtained results reveal that genetically-controlled secretion of biofilm protein components may lead to the rational tuning of Young’s moduli of biofilms as promising candidates at the bionano interface.
      Keywords
      Atomic force microscopy
      Biofilms
      Escherichia coli
      Glycoproteins
      Mechanical properties
      Nanofibers
      Bacterial biofilm
      Bio-nano interfaces
      Biochemical properties
      Escherichia coli (E. coli)
      Force spectroscopy
      Protein components
      Protein composition
      Protein nanofibers
      Proteins
      Permalink
      http://hdl.handle.net/11693/37291
      Published Version (Please cite this version)
      https://doi.org/10.1021/acs.langmuir.7b00112
      Collections
      • Department of Mechanical Engineering 277
      • Institute of Materials Science and Nanotechnology (UNAM) 1863
      • Nanotechnology Research Center (NANOTAM) 1039
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