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. 2014 Mar 11;15(3):4299–4317. doi: 10.3390/ijms15034299

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© 2014 by the authors; licensee MDPI, Basel, Switzerland

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Figure 1. — (A) Schematic showing the attachment of RGD on TiO₂ nanogratings; (B) 3-D AFM images showing retention of the TiO₂ nanopatterns after RGD immobilization; (C) Time-of-Flight Secondary Ion Mass Spectrometry (ToF-SIMS) confirmed the attachment of RDG peptide on the TiO₂ surface. The specific fragment pattern generated by removal of individual amino acids from peptide is shown in the lower panels. (Glycine m/z 30.04 u:CH₄N⁺, Arginine m/z 100.07 u:C₄H₁₀N⁺, Aspartic acid m/z 88.08 u:C₃H₆NO₂⁺); (D) Typical peak ratio of amino acids normalized by total ions; (E) XPS spectra; wide scan of N1s spectra of TiO₂ surfaces before and after the immobilization of peptide. Inset: a high-resolution scan of N1s.

Figure 1. — (A) Schematic showing the attachment of RGD on TiO₂ nanogratings; (B) 3-D AFM images showing retention of the TiO₂ nanopatterns after RGD immobilization; (C) Time-of-Flight Secondary Ion Mass Spectrometry (ToF-SIMS) confirmed the attachment of RDG peptide on the TiO₂ surface. The specific fragment pattern generated by removal of individual amino acids from peptide is shown in the lower panels. (Glycine m/z 30.04 u:CH₄N⁺, Arginine m/z 100.07 u:C₄H₁₀N⁺, Aspartic acid m/z 88.08 u:C₃H₆NO₂⁺); (D) Typical peak ratio of amino acids normalized by total ions; (E) XPS spectra; wide scan of N1s spectra of TiO₂ surfaces before and after the immobilization of peptide. Inset: a high-resolution scan of N1s.