Mauquoy, Sara
[UCL]
Dupont-Gillain, Christine C.
[UCL]
Layer-by-layer (LbL) assembly is a surface modification method which may bring complexity to bioint-erfaces designed to control cell-material interactions. This work aims at investigating the LbL assemblyof two extracellular matrix proteins, collagen (Col) and fibronectin (Fn), on polystyrene substrates. LbLassembly, which is widely applied to polyelectrolytes, is not easily transferred to proteins. Differentbuffers and conditions are tested, and LbL assembly is compared to the simultaneous adsorption of Fnand Col. Build-up and properties of the films are monitored using quartz crystal microbalance, ellipsom-etry, water contact angle measurements, and atomic force microscopy. Results show that denatured Colleads to smoother films, and that the addition of a polyethyleneimine anchoring layer increases filmthickness. A more regular construction and thicker films are obtained with Hepes (pH 7.4) compared toother buffers. However, the LbL assembly is not sustainable and stops after the deposition of a few layers.Films obtained by simultaneous adsorption have lower water contact angles, different morphologies,lower water content and are as thick or thicker compared to the ones prepared by the LbL method. Thepresent work shows that collagen and fibronectin are not involved in a true LbL assembly process. Theobtained biointerfaces however exhibit different properties compared to those obtained by the one-stepadsorption of these proteins. These differences could be exploited to control cell fate.
Bibliographic reference |
Mauquoy, Sara ; Dupont-Gillain, Christine C.. Combination of collagen and fibronectin to design biomimetic interfaces: do these proteins form layer-by-layer assemblies?. In: Colloids and Surfaces B: Biointerfaces, Vol. 147, p. 54-64 (2016) |
Permanent URL |
http://hdl.handle.net/2078.1/176198 |