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

作者：Salvagni Emiliano^*; Berguig Geoffrey; Engel Elisabeth; Carlos Rodriguez Cabello J; Coullerez Geraldine; Textor Marcus; Planell Josep A; Javier Gil F; Aparicio Conrado

来源：Colloids and Surfaces B: Biointerfaces , 2014, 114: 225-233.

DOI：10.1016/j.colsurfb.2013.10.008

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

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.

• 出版日期2014-2-1