http://www.cnr.it/ontology/cnr/individuo/prodotto/ID244148
Self-Assembly of Hydrophobin Protein Rodlets Studied with Atomic Force Spectroscopy in Dynamic Mode (Articolo in rivista)
- Type
- Label
- Self-Assembly of Hydrophobin Protein Rodlets Studied with Atomic Force Spectroscopy in Dynamic Mode (Articolo in rivista) (literal)
- Anno
- 2012-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/la2028093 (literal)
- Alternative label
S. Houmadi+??, Raul D. Rodriguez+§?, S. Longobardi?, P. Giardina?, M. C. Faure+, M. Giocondo ?, and E. Lacaze+? (2012)
Self-Assembly of Hydrophobin Protein Rodlets Studied with Atomic Force Spectroscopy in Dynamic Mode
in Langmuir; ACS, American chemical society, Washington, DC (Stati Uniti d'America)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- S. Houmadi+??, Raul D. Rodriguez+§?, S. Longobardi?, P. Giardina?, M. C. Faure+, M. Giocondo ?, and E. Lacaze+? (literal)
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- http://biblioproxy.cnr.it:2054/doi/pdf/10.1021/la2028093 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- +CNRS, UMR7588, Institut des Nano-Sciences de Paris (INSP), 4 place Jussieu 75005 PARIS, France
?CNR-IPCF - UOS di Cosenza. c/o Dipartimento di Fisica, Universita della Calabria, 87036 Rende, Italy
? UPMC Univ Paris 06, UMR 7588, Institut des Nano-Sciences de Paris (INSP), 4 Place Jussieu, F-75005 Paris, France
§ Institute of Physics, Chemnitz University of Technology, 09107 Chemnitz, Germany
? Dipartimento di Chimica Organica e Biochimica, Universita di Napoli Federico II, Via Cintia 4, 80126 Napoli, Italy (literal)
- Titolo
- Self-Assembly of Hydrophobin Protein Rodlets Studied with Atomic Force Spectroscopy in Dynamic Mode (literal)
- Abstract
- We have investigated the self-assembling properties of the class I hydrophobin Vmh2 isolated from the fungus Pleurotus ostreatus. Five different hydrophobin self assembled samples including monolayers, bilayers, and rodlets have been prepared by Langmuir technique and studied at the nanoscale. Local wettability and visco-elasticity of the different hydrophobins samples were obtained from atomic force spectroscopy experiments in dynamic mode performed at different, controlled relative humidity (RH) values. It was found that hydrophobins assembled either in rodlets or in bilayer films, display similar hydropathicity and viscoelasticity in contrast to the case of monolayers, whose hydropathicity and viscoelasticity depend on the adopted preparation method (Langmuir-Blodgett or Langmui-Schaeffer). The comparison with monolayers properties evidences a rearrangement of the bilayers adsorbed onto solid substrates. It is shown that this rearrangement leads to the formation of a stable hydrophobic film, and that the rodlets structure consists in fragments of restructured proteins bilayers. Our results support the hypothesis that the observed variations in the viscoelastic properties could be ascribed to the localization of the large flexible loop, typical of Class I hydrophobins which appears free at the air interface for LB monolayers but not for the other samples. These findings should now serve future developments and applications of hydrophobin films beyond the archetypal monolayer. (literal)
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