Adsorption of tripeptide RGD on rutile TiO2 nanotopography surface in aqueous solution

Aqueous Peptide–TiO2 Interfaces: Isoenergetic Binding via Either Entropically or Enthalpically Driven Mechanisms

“…5,17 Therefore, the investigation of entire peptide chains in contact with inorganic surfaces is a critical component in advancing our understanding. 26 The tripeptide motif RGD and its interaction with titania surfaces has been of particular interest, [27][28][29][30][31][32][33] while others have sought to isolate and identify TiO2-binding peptides using biocombinatorial techniques to gain a deeper understanding of which peptide characteristics can confer strong titania-binding affinity. 32,[34][35][36][37] A crucial next step in advancing our understanding is the careful characterization of the adsorption of materials-binding peptides at aqueous titania interfaces.…”

Selective binding of oligonucleotide on TiO 2 surfaces modified by swift heavy ion beam lithography

“…Cleaves et al [14] pointed out that the binding capacity of nucleotides with surface functional groups on rutile is promoted at kink and steps sites on the surface. Such defects behave as islands with different chemical behaviour compared to a defect free surface [15]. It is also known that TiO 2 surfaces change their chemical and physical properties by UV irradiation.…”

“…Furthermore, experimental studies describe the direct adsorption of DNA oligonucleotides to anatase TiO 2 nanoparticles [13] and mineral rutile TiO 2 [14]. Theoretical approaches highlight the relevance of the surface chemical properties for the absorption of tripeptides on TiO 2 rutile single crystal [15]. Since the surface characteristics of TiO 2 play a key role in the interaction with biomolecules and cells, new processes for generating controllable changes of TiO 2 surface properties, such as topography, morphology and surface chemistry, can be advantageous in biosensing and 3 dimensional (3D) cellular scaffolding [16] applications for near future analytical, diagnostics, and imaging techniques.…”

Molecular simulations of myoglobin adsorbed on rutile (110) and (001) surfaces

“…They [17] also studied the effect of Na + on peptide adsorption. Song et al [18] investigated the adsorption mechanisms of Arg-Gly-Asp on the nanotopography and perfect rutile TiO 2 (1 1 0) surface. The surface structure of TiO 2 has a stronger influence on local surface chemistry as compared with metals or elemental semiconductors.…”