elastin has been researched along with 3-(4-carboxybenzoyl)-2-quinolinecarboxaldehyde* in 1 studies
1 other study(ies) available for elastin and 3-(4-carboxybenzoyl)-2-quinolinecarboxaldehyde
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A bioactive elastin-like recombinamer reduces unspecific protein adsorption and enhances cell response on titanium surfaces.
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. Topics: Adsorption; Alkaline Phosphatase; Benzoates; Cell Adhesion; Cell Differentiation; Cell Proliferation; Coated Materials, Biocompatible; Elastin; Humans; L-Lactate Dehydrogenase; Materials Testing; Mesenchymal Stem Cells; Photoelectron Spectroscopy; Quinolines; Recombinant Proteins; Surface Properties; Titanium | 2014 |