http://www.cnr.it/ontology/cnr/individuo/prodotto/ID14231
Surface immobilization of fibronectin-derived PHSRN peptide on functionalized polymer film - Effects on fibroblast spreading (Articolo in rivista)
- Type
- Label
- Surface immobilization of fibronectin-derived PHSRN peptide on functionalized polymer film - Effects on fibroblast spreading (Articolo in rivista) (literal)
- Anno
- 2010-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.jcis.2009.09.046 (literal)
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- C. Satriano; G.M.L. Messina; C. Marino; I. Aiello; E. Conte; D. La Mendola; D. Distefano; F. D'Alessandro; G. Pappalardo; G. Impellizzeri. (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Cristina Satriano, Department of Chemical Sciences, Catania University, Italy
Grazia M.L. Messina, Department of Chemical Sciences, Catania University, Italy
Clara Marino, Department of Chemical Sciences, Catania University, Italy
Ivana Aiello, Department of Chemical Sciences, Catania University, Italy
Enrico Conte, Department of Chemical Sciences, Catania University, Italy
Donatella A. Distefano, Department of Chemical Sciences, Catania University, Italy
Franca D'Alessandro, Department of Chemical Sciences, Catania University, Italy
Giuseppe Impellizzeri, Department of Chemical Sciences, Catania University, Italy (literal)
- Titolo
- Surface immobilization of fibronectin-derived PHSRN peptide on functionalized polymer film - Effects on fibroblast spreading (literal)
- Abstract
- The Pro-His-Ser-Arg-Asn (PHSRN) sequence in fibronectin is a second cell-binding site that synergistically affects Arg-Gly-Asp (RGD). The PHSRN peptide also induces cell invasion and accelerates wound healing. We report on the surface immobilization of PHSRN by spontaneous adsorption on polysiloxane thin films which have different surface free energy characteristics. Low-surface energy (hydrophobic) polysiloxane and the corresponding high-surface energy (hydrophilic) surfaces obtained by UV-ozone treatments were used as adsorbing substrates. The peptide adsorption process was investigated by quartz crystal microbalance with dissipation monitoring and atomic force microscopy. Both adsorption kinetics and peptide rearrangement dynamics at the solid interface were significantly different on the surface-modified films compared to the untreated ones. Fibroblast cells cultures at short times and in a simplified environment, i.e., a medium-free solution, were prepared to distinguish interaction events at the interface between cell membrane and surface-immobilized peptide for the two cases. It turned out that the cell-adhesive effect of immobilized PHSRN was different for hydrophobic compared to hydrophilic ones. Early signatures of cell spreading were only observed on the hydrophilic substrates. These effects are explained in terms of different spatial arrangements of PHSRN molecules immobilized on the two types of surfaces. (literal)
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