A synthetically modified hydrophobin showing enhanced fluorous affinity

Research output: Contribution to journalArticle


  • Roberto Milani
  • Lisa Pirrie
  • Lara Gazzera
  • Arja Paananen
  • Michele Baldrighi
  • Evanthia Monogioudi
  • Gabriella Cavallo
  • Markus Linder

  • Giuseppe Resnati
  • Pierangelo Metrangolo

Research units

  • VTT Technical Research Centre of Finland
  • Italian Institute of Technology
  • Polytechnic University of Milan


Hydrophobins are natural surfactant proteins endowed with exceptional surface activity and film-forming capabilities and their use as effective “fluorine-free fluorosurfactants” has been recently reported. In order to increase their fluorophilicity further, here we report the preparation of a unique fluorous-modified hydrophobin, named F-HFBI. F-HFBI was found to be more effective than its wild-type parent protein HFBI at reducing interface tension of water at both air/water and oil/water interfaces, being particularly effective at the fluorous/water interface. F-HFBI was also found to largely retain the exceptionally good capability of forming strong and elastic films, typical of the hydrophobin family. Further studies by interface shear rheology and isothermal compression, alongside Quartz Crystal Microbalance and Atomic Force Microscopy, demonstrated the tendency of F-HFBI to form thicker films compared to the wild-type protein. These results suggest that F-HFBI may function as an effective compatibilizer for biphasic systems comprising a fluorous phase.


Original languageEnglish
Pages (from-to)140-147
Number of pages8
JournalJournal of Colloid and Interface Science
Publication statusPublished - 15 Jun 2015
MoE publication typeA1 Journal article-refereed

    Research areas

  • Hydrophobin, Surfactant protein, Protein film formation, Fluorinated material, Fluorous tag, Compatibilization

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