| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 599664 | Colloids and Surfaces B: Biointerfaces | 2014 | 6 Pages |
•The adsorption mechanism of titanium-binding peptide (TBP) on metal oxide substrates was investigated.•A positively charged amino acid, lysine (K) or arginine (R), in TBP is the primary factor in adsorption on metal oxide substrates.•The adsorption force of K is stronger than R, although R reportedly is the main contributor to adsorption.•Selective adsorption of ferritins was achieved by alanine-substituted TBP in the absence of a surfactant used in conventional selective adsorption.
The adsorption mechanism of titanium-binding peptide (TBP) on metal oxide substrates was investigated by evaluating the adsorption behavior of ferritins with various alanine-substituted TBPs. Results revealed that (a) a positively charged amino acid, lysine (K) or arginine (R), in TBP can anchor ferritin to negative zeta-potential substrates, (b) the adsorption force of K is stronger than R, and (c) local electrostatic interactions and flexibility of TBP directly affect adsorption. Based on these findings, selective ferritin adsorption on SiO2 with TiOX patterned surfaces in a surfactant-free condition was demonstrated. Alanine-substituted TBP with one positively charged amino acid (K) and one negatively charged amino acid (D), achieved ferritin-selective adsorption without a surfactant. The importance of controlled electrostatic forces between TBP and a substrate for selective adsorption without a surfactant was clearly demonstrated.
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