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Colloids Surf B Biointerfaces. 2014 Feb 1;114:225-33. doi: 10.1016/j.colsurfb.2013.10.008. Epub 2013 Oct 17.

A bioactive elastin-like recombinamer reduces unspecific protein adsorption and enhances cell response on titanium surfaces.

Author information

1
Nanoengineering Research Centre (CRnE), Biomaterials, Biomechanics and Tissue Engineering Group (BiBiTE), Technical University of Catalonia (UPC), Barcelona, Spain. Electronic address: emiliano.salvagni@gmail.com.
2
Nanoengineering Research Centre (CRnE), Biomaterials, Biomechanics and Tissue Engineering Group (BiBiTE), Technical University of Catalonia (UPC), Barcelona, Spain; Department of Bioengineering, University of Washington, Seattle, WA, USA.
3
Institute for Bioengineering of Catalonia (IBEC), Barcelona, Spain.
4
G.I.R. BIOFORGE, CIBER-BBN, Universidad de Valladolid, Valladolid, Spain.
5
Laboratory for Surface Science and Technology, Swiss Federal Institute of Technology (ETH), Zürich, Switzerland.
6
Nanoengineering Research Centre (CRnE), Biomaterials, Biomechanics and Tissue Engineering Group (BiBiTE), Technical University of Catalonia (UPC), Barcelona, Spain.
7
Nanoengineering Research Centre (CRnE), Biomaterials, Biomechanics and Tissue Engineering Group (BiBiTE), Technical University of Catalonia (UPC), Barcelona, Spain; MDRCBB-Minnesota Dental Research Center for Biomaterials and Biomechanics, University of Minnesota School of Dentistry, Minneapolis, MN, USA. Electronic address: apari003@umn.edu.

Abstract

We present the immobilization on synthetic substrates of elastin-like recombinamers (ELR) that combine a bioactive motif for cell adhesion with protein antifouling properties. Physical adsorption of the recombinamers and covalent-grafting through organosilane chemistry were investigated. The biochemically-modified surfaces were thoroughly characterized and tested for protein absorption in serum by fluorescence-labelling, XPS, Ellipsometry, and OWLS. The ELR were successfully grafted and stable, even upon mechanical stresses; being the covalent bonding favourable over physical adsorption. The coated metal surfaces exhibited excellent reduction of serum protein adsorption (9 ng/cm(2)) compared to the bare metal surface (310 ng/cm(2)). Non-specific protein adsorption may mask the introduced bioactive motifs; therefore, the bioactivated surfaces should display serum-protein antifouling properties. Finally, improved hMSCs response was assessed on the bioactivated substrates. In summary, the coatings simultaneously displayed anti-fouling and bioactive properties. These studies investigated key factors to enhance tissue material interactions fundamental for the design of bioactive devices and future biomedical applications.

KEYWORDS:

Bioactivity; Biofunctionalization; Biomimetic; Cell response; Protein immobilization; Protein resistance

PMID:
24200950
DOI:
10.1016/j.colsurfb.2013.10.008
[Indexed for MEDLINE]

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