期刊
LANGMUIR
卷 34, 期 21, 页码 6010-6020出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.langmuir.8b00441
关键词
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资金
- Grant Agency of the Czech Republic (GACR) [16-02702S]
- European Regional Development Fund OPPK [CZ.2.16/3.1.00/21545]
- Ministry of Health of the Czech Republic [16-30544A]
Polymer layers capable of suppressing protein adsorption from biological media while presenting extracellular matrix-derived peptide motifs offer valuable new options for biomimetic surface engineering. Herein, we provide detailed insights into physicochemical changes induced in a nonfouling poly(ethylene oxide) (PEO) brush/polydopamine (PDA) system by incorporation of adhesion ligand (RGD) peptides. Brushes with high surface chain densities (sigma >= 0.5 chains-nm(-2)) and pronounced hydrophilicity (water contact angles <= 10 degrees) were prepared by end tethering of heterobifunctional PEOs (M-n approximate to 20 000 g.mol(-1)) to PDA-modified surfaces from a reactive melt. Using alkyne distal end group on the PEO chains, azidopentanoic-bearing peptides were coupled through a copper-catalyzed Huisgen azide-alkyne click cycloaddition reaction. The surface concentration of RGD was tuned from complete saturation of the PEO surface with peptides (1.7 X 10(5) fmol.cm(-2)) to values which may induce distinct differences in cell adhesion (<6.0 x 10(2) fmol.cm(-2)). Infrared reflection absorption and X-ray photoelectron spectroscopies proved the PDA-PEO layers covalent structure and the immobilization of RGD peptides. The complete reconstruction of experimental electrohydrodynamics data utilizing mean-field theory predictions further verified the attained brush structure of the end-tethered PEO chains which provided hydrodynamic screening of the PDA anchor. Increasing the surface concentration of immobilized RGD peptides led to increased interfacial charging. Supported by simulations, this observation was attributed to the ionization of functional groups in the amino acid sequence and to the pH-dependent adsorption of water ions (OH- > H3O+) from the electrolyte. Despite the distinct differences observed in the electrokinetic analysis of the surfaces bearing different amounts of RGD, it was found that the peptide presence on PEO(20 000)-PDA layers does not have a significant effect on the nonfouling properties of the system. Notably, the presented PEO(20 000)-PDA layers bearing RGD peptides in the surface concentration range 5.9 to 1.7 X 10(5) fmol.cm(-2) reduced the protein adsorption from fetal bovine serum to less than 30 ng.cm(-2), that is, values comparable to the ones obtained for pristine PEO(20 000)-PDA layers.
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