This work was supported by the Ligue contre le Cancer (Région Alsace). N.J. is indebted to the Faculté de Chirurgie Dentaire of Strasbourg for financial support. The authors are indebted to Marion Dussaussois and Géraldine Greiner for their contribution to the QCMD measurements. The authors also thank Jerôme Mutterer (Institut de Biologie Moléculaire des Plantes, Strasbourg, France) for assistance with the CLSM. The CLSM platform used in this study was co-financed by the Région Alsace, the CNRS, the Université Louis Pasteur, and the Association pour la Recherche sur le Cancer. This work was supported by the program ACI “Nanosciences” (NR204) from the Ministère Français Déligué à la Recherche.
Short-Time Tuning of the Biological Activity of Functionalized Polyelectrolyte Multilayers†
Article first published online: 23 MAR 2005
Copyright © 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Advanced Functional Materials
Volume 15, Issue 4, pages 648–654, April, 2005
How to Cite
Benkirane-Jessel, N., Lavalle, P., Hübsch, E., Holl, V., Senger, B., Haïkel, Y., Voegel, J.-C., Ogier, J. and Schaaf, P. (2005), Short-Time Tuning of the Biological Activity of Functionalized Polyelectrolyte Multilayers. Adv. Funct. Mater., 15: 648–654. doi: 10.1002/adfm.200400129
- Issue published online: 23 MAR 2005
- Article first published online: 23 MAR 2005
- Manuscript Accepted: 11 AUG 2004
- Manuscript Received: 26 MAR 2004
- Bioactive materials;
- Layer-by-layer assembly;
This article demonstrates the tuning of the biological activity of a surface functionalized by a polyelectrolyte multilayer. The interaction of protein A with macrophages is used as the model system. The film consists of two polypeptides, poly(lysine) and poly(glutamic acid); each “build-up” solution is a mixture of the respective D- and L-enantiomers (d and l enantiomers). Cells are deposited on top of the film, and they produce tumor necrosis factor alpha (TNF-α) as they come into contact with the protein. Depending upon the d/l-enantiomer ratio of the polyelectrolyte solutions used for the film build-up, and the embedding depth of the protein, the production of TNF-α commences after a varying induction time and displays a transition from no-production to full-production, which takes place over a period of time that depends on the film's composition and embedding depth. Thus, it is shown that by changing these two parameters the timing of the protein's activity can be accurately tuned.