A synthetically modified hydrophobin showing enhanced fluorous affinity

Roberto Milani, Lisa Pirrie, Lara Gazzera, Arja Paananen, Michele Baldrighi, Evanthia Monogioudi, Gabriella Cavallo, Markus Linder, Giuseppe Resnati, Pierangelo Metrangolo

Research output: Contribution to journalArticleScientificpeer-review

7 Citations (Scopus)

Abstract

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
JournalJournal of Colloid and Interface Science
Volume448
DOIs
Publication statusPublished - 2015
MoE publication typeA1 Journal article-refereed

Fingerprint

Proteins
Water
Compatibilizers
Quartz crystal microbalances
Rheology
Fluorine
Thick films
Surface tension
Atomic force microscopy
Surface active agents
Surface-Active Agents
1-(heptafluorobutyryl)imidazole
Oils
Air

Keywords

  • hydrophobin
  • surfactant protein
  • protein film formation
  • fluorinated material
  • fluorous tag
  • compatibilization

Cite this

Milani, Roberto ; Pirrie, Lisa ; Gazzera, Lara ; Paananen, Arja ; Baldrighi, Michele ; Monogioudi, Evanthia ; Cavallo, Gabriella ; Linder, Markus ; Resnati, Giuseppe ; Metrangolo, Pierangelo. / A synthetically modified hydrophobin showing enhanced fluorous affinity. In: Journal of Colloid and Interface Science. 2015 ; Vol. 448. pp. 140-147.
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author = "Roberto Milani and Lisa Pirrie and Lara Gazzera and Arja Paananen and Michele Baldrighi and Evanthia Monogioudi and Gabriella Cavallo and Markus Linder and Giuseppe Resnati and Pierangelo Metrangolo",
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Milani, R, Pirrie, L, Gazzera, L, Paananen, A, Baldrighi, M, Monogioudi, E, Cavallo, G, Linder, M, Resnati, G & Metrangolo, P 2015, 'A synthetically modified hydrophobin showing enhanced fluorous affinity', Journal of Colloid and Interface Science, vol. 448, pp. 140-147. https://doi.org/10.1016/j.jcis.2015.02.003

A synthetically modified hydrophobin showing enhanced fluorous affinity. / Milani, Roberto; Pirrie, Lisa; Gazzera, Lara; Paananen, Arja; Baldrighi, Michele; Monogioudi, Evanthia; Cavallo, Gabriella; Linder, Markus; Resnati, Giuseppe; Metrangolo, Pierangelo.

In: Journal of Colloid and Interface Science, Vol. 448, 2015, p. 140-147.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - A synthetically modified hydrophobin showing enhanced fluorous affinity

AU - Milani, Roberto

AU - Pirrie, Lisa

AU - Gazzera, Lara

AU - Paananen, Arja

AU - Baldrighi, Michele

AU - Monogioudi, Evanthia

AU - Cavallo, Gabriella

AU - Linder, Markus

AU - Resnati, Giuseppe

AU - Metrangolo, Pierangelo

N1 - Project code: 100495 Project code: 101066

PY - 2015

Y1 - 2015

N2 - 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.

AB - 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.

KW - hydrophobin

KW - surfactant protein

KW - protein film formation

KW - fluorinated material

KW - fluorous tag

KW - compatibilization

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DO - 10.1016/j.jcis.2015.02.003

M3 - Article

VL - 448

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JO - Journal of Colloid and Interface Science

JF - Journal of Colloid and Interface Science

SN - 0021-9797

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