How to cite this article: Vadillo-Rodríguez V, Pacha-Olivenza MA, Gónzalez-Martín ML, Bruque JM, Gallardo-Moreno AM. 2013. Adsorption behavior of human plasma fibronectin on hydrophobic and hydrophilic Ti6Al4V substrata and its influence on bacterial adhesion and detachment. J Biomed Mater Res Part A 2013:101A:1397–1404.
Adsorption behavior of human plasma fibronectin on hydrophobic and hydrophilic Ti6Al4V substrata and its influence on bacterial adhesion and detachment†
Version of Record online: 18 OCT 2012
Copyright © 2012 Wiley Periodicals, Inc.
Journal of Biomedical Materials Research Part A
Volume 101A, Issue 5, pages 1397–1404, May 2013
How to Cite
Vadillo-Rodríguez, V., Pacha-Olivenza, M. A., Gónzalez-Martín, M. L., Bruque, J. M. and Gallardo-Moreno, A. M. (2013), Adsorption behavior of human plasma fibronectin on hydrophobic and hydrophilic Ti6Al4V substrata and its influence on bacterial adhesion and detachment. J. Biomed. Mater. Res., 101A: 1397–1404. doi: 10.1002/jbm.a.34447
- Issue online: 25 MAR 2013
- Version of Record online: 18 OCT 2012
- Manuscript Accepted: 5 SEP 2012
- Manuscript Revised: 19 AUG 2012
- Manuscript Received: 9 JUL 2012
- Ministerio de Ciencia e Innovación. Grant Number: RYC-2008-03482
- Ministerio de Ciencia e Innovación. Grant Number: MAT2009-14695-C04-01
- Junta of Extremadura. Grant Number: PRI08A124
- titanium alloy;
- protein adsorption;
- bacterial adhesion
Biomaterial implant-associated infections, a common cause of medical devices' failure, are initiated by bacterial adhesion to an adsorbed protein layer on the implant material surface. In this study, the influence of protein surface orientation on bacterial adhesion has been examined using three clinically relevant bacterial strains known to express specific binding sites for human plasma fibronectin (HFN). HFN was allowed to adsorb on hydrophobic Ti6Al4V and physically modified hydrophilic Ti6Al4V substrata. Ellipsometric data reveal that the characteristics of the adsorbed protein layers primary depend on solid surface tension and the initial protein concentration in solution. In particular, HFN molecules adopt a more extended conformation on hydrophobic than hydrophilic surfaces, an effect that is more pronounced at low than at high initial protein concentrations. Moreover, the extended conformation of the protein molecules on these surfaces likely facilitates the exposure of specific sites for adhesion, resulting in the higher bacterial-cell attachment observed regardless of the strain considered. Contact angle measurements and the analysis of the number of remaining adhering cells after being subjected to external forces further suggest that both specific and nonspecific (hydrophobic) interactions play an important role on bacterial attachment. This study is the first one to evaluate the influence of surface hydrophobicity on protein adsorption and its subsequent effect on bacterial adhesion using a material whose hydrophobicity was not modified using chemical treatments that potentially led to surface properties changes other than hydrophobicity. © 2012 Wiley Periodicals, Inc. J Biomed Mater Res Part A, 2013.